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LongText Report for: 1YSC-pdb

Name Class
1YSC-pdb
HEADER    HYDROLASE(CARBOXYPEPTIDASE)             08-MAR-94   1YSC      1YSC   2
COMPND    SERINE CARBOXYPEPTIDASE (CPY, CPD-Y, OR PROTEINASE C)         1YSC   3
COMPND   2 (E.C.3.4.16.5)                                               1YSC   4
SOURCE    YEAST (SACCHAROMYCES CEREVISIAE)                              1YSC   5
AUTHOR    J.A.ENDRIZZI,S.J.REMINGTON                                    1YSC   6
REVDAT   1   22-JUN-94 1YSC    0                                        1YSC   7
JRNL        AUTH   J.A.ENDRIZZI,K.BREDDAM,S.J.REMINGTON                 1YSC   8
JRNL        TITL   2.8 ANGSTROMS STRUCTURE OF YEAST SERINE              1YSC   9
JRNL        TITL 2 CARBOXYPEPTIDASE                                     1YSC  10
JRNL        REF    TO BE PUBLISHED   REF NOW ASSIGNED AS                1YSC  11
JRNL        REFN                                                  0353  1YSC  12
REMARK   1                                                              1YSC  13
REMARK   2                                                              1YSC  14
REMARK   2 RESOLUTION. 2.8  ANGSTROMS.                                  1YSC  15
REMARK   3                                                              1YSC  16
REMARK   3 REFINEMENT.                                                  1YSC  17
REMARK   3   PROGRAM                    TNT                             1YSC  18
REMARK   3   AUTHORS                    TRONRUD,TEN EYCK,MATTHEWS       1YSC  19
REMARK   3   R VALUE                    0.162                           1YSC  20
REMARK   3   RMSD BOND DISTANCES        0.16   ANGSTROMS                1YSC  21
REMARK   3   RMSD BOND ANGLES           2.75   DEGREES                  1YSC  22
REMARK   3                                                              1YSC  23
REMARK   3   NUMBER OF PROTEIN ATOMS                       3253         1YSC  24
REMARK   3   NUMBER OF SOLVENT ATOMS                         38         1YSC  25
REMARK   4                                                              1YSC  26
REMARK   4 IN *SITE RECORDS BELOW, CAT REFERS TO CATALYTIC RESIDUES,    1YSC  27
REMARK   4 CBS REFERS TO CARBOXYLATE BINDING SITE, S1P REFERS TO A      1YSC  28
REMARK   4 S1' SUBSITE (BINDS C-TERMINAL SIDE CHAIN), AND S1S REFERS    1YSC  29
REMARK   4 TO A S1 SUBSITE (BINDS PENULTIMATE SIDE CHAIN).              1YSC  30
REMARK   5                                                              1YSC  31
REMARK   5 THE SHEET STRUCTURE OF THIS MOLECULE IS BIFURCATED.  IN      1YSC  32
REMARK   5 ORDER TO REPRESENT THIS FEATURE IN THE SHEET RECORDS BELOW,  1YSC  33
REMARK   5 TWO SHEETS ARE DEFINED.  STRANDS 1, 2, 3, 5, 6, 7, 8, 9, 10  1YSC  34
REMARK   5 AND 11 OF S1A AND S1B ARE IDENTICAL.                         1YSC  35
REMARK   6                                                              1YSC  36
REMARK   6 SOME SURFACE LOOPS ARE POORLY DEFINED AND HAVE HIGH          1YSC  37
REMARK   6 B-VALUES, INCLUDING RESIDUES 1 - 17, 23 - 26, 105 - 108,     1YSC  38
REMARK   6 134 - 138, 263 - 266, 282 - 286, 375 - 376.                  1YSC  39
REMARK   6                                                              1YSC  40
REMARK   6 PDB ADVISORY NOTICE:                                         1YSC  41
REMARK   6 RESIDUES ILE 71, ILE 275, ILE 302 AND ILE 415 HAVE           1YSC  42
REMARK   6 CHIRALITY PROBLEM.                                           1YSC  43
REMARK   7                                                              1YSC  44
REMARK   7 SIDE CHAIN ATOMS OF RESIDUES ARE MISSING BECAUSE THE         1YSC  45
REMARK   7 ELECTRON DENSITY WAS ILL-DEFINED.                            1YSC  46
SEQRES   1    421  LYS ILE LYS ASP PRO LYS ILE LEU GLY ILE ASP PRO ASN  1YSC  47
SEQRES   2    421  VAL THR GLN TYR THR GLY TYR LEU ASP VAL GLU ASP GLU  1YSC  48
SEQRES   3    421  ASP LYS HIS PHE PHE PHE TRP THR PHE GLU SER ARG ASN  1YSC  49
SEQRES   4    421  ASP PRO ALA LYS ASP PRO VAL ILE LEU TRP LEU ASN GLY  1YSC  50
SEQRES   5    421  GLY PRO GLY CYS SER SER LEU THR GLY LEU PHE PHE GLU  1YSC  51
SEQRES   6    421  LEU GLY PRO SER SER ILE GLY PRO ASP LEU LYS PRO ILE  1YSC  52
SEQRES   7    421  GLY ASN PRO TYR SER TRP ASN SER ASN ALA THR VAL ILE  1YSC  53
SEQRES   8    421  PHE LEU ASP GLN PRO VAL ASN VAL GLY PHE SER TYR SER  1YSC  54
SEQRES   9    421  GLY SER SER GLY VAL SER ASN THR VAL ALA ALA GLY LYS  1YSC  55
SEQRES  10    421  ASP VAL TYR ASN PHE LEU GLU LEU PHE PHE ASP GLN PHE  1YSC  56
SEQRES  11    421  PRO GLU TYR VAL ASN LYS GLY GLN ASP PHE HIS ILE ALA  1YSC  57
SEQRES  12    421  GLY GLU SER TYR ALA GLY HIS TYR ILE PRO VAL PHE ALA  1YSC  58
SEQRES  13    421  SER GLU ILE LEU SER HIS LYS ASP ARG ASN PHE ASN LEU  1YSC  59
SEQRES  14    421  THR SER VAL LEU ILE GLY ASN GLY LEU THR ASP PRO LEU  1YSC  60
SEQRES  15    421  THR GLN TYR ASN TYR TYR GLU PRO MET ALA CYS GLY GLU  1YSC  61
SEQRES  16    421  GLY GLY GLU PRO SER VAL LEU PRO SER GLU GLU CYS SER  1YSC  62
SEQRES  17    421  ALA MET GLU ASP SER LEU GLU ARG CYS LEU GLY LEU ILE  1YSC  63
SEQRES  18    421  GLU SER CYS TYR ASP SER GLN SER VAL TRP SER CYS VAL  1YSC  64
SEQRES  19    421  PRO ALA THR ILE TYR CYS ASN ASN ALA GLN LEU ALA PRO  1YSC  65
SEQRES  20    421  TYR GLN ARG THR GLY ARG ASN VAL TYR ASP ILE ARG LYS  1YSC  66
SEQRES  21    421  ASP CYS GLU GLY GLY ASN LEU CYS TYR PRO THR LEU GLN  1YSC  67
SEQRES  22    421  ASP ILE ASP ASP TYR LEU ASN GLN ASP TYR VAL LYS GLU  1YSC  68
SEQRES  23    421  ALA VAL GLY ALA GLU VAL ASP HIS TYR GLU SER CYS ASN  1YSC  69
SEQRES  24    421  PHE ASP ILE ASN ARG ASN PHE LEU PHE ALA GLY ASP TRP  1YSC  70
SEQRES  25    421  MET LYS PRO TYR HIS THR ALA VAL THR ASP LEU LEU ASN  1YSC  71
SEQRES  26    421  GLN ASP LEU PRO ILE LEU VAL TYR ALA GLY ASP LYS ASP  1YSC  72
SEQRES  27    421  PHE ILE CYS ASN TRP LEU GLY ASN LYS ALA TRP THR ASP  1YSC  73
SEQRES  28    421  VAL LEU PRO TRP LYS TYR ASP GLU GLU PHE ALA SER GLN  1YSC  74
SEQRES  29    421  LYS VAL ARG ASN TRP THR ALA SER ILE THR ASP GLU VAL  1YSC  75
SEQRES  30    421  ALA GLY GLU VAL LYS SER TYR LYS HIS PHE THR TYR LEU  1YSC  76
SEQRES  31    421  ARG VAL PHE ASN GLY GLY HIS MET VAL PRO PHE ASP VAL  1YSC  77
SEQRES  32    421  PRO GLU ASN ALA LEU SER MET VAL ASN GLU TRP ILE HIS  1YSC  78
SEQRES  33    421  GLY GLY PHE SER LEU                                  1YSC  79
FTNOTE   1                                                              1YSC  80
FTNOTE   1 CIS PROLINE - PRO      54                                    1YSC  81
FTNOTE   2                                                              1YSC  82
FTNOTE   2 CIS PROLINE - PRO      96                                    1YSC  83
FTNOTE   3                                                              1YSC  84
FTNOTE   3 RESIDUE NAG 871 HAS STRONGER ELECTRON DENSITY BETWEEN IT     1YSC  85
FTNOTE   3 AND ASN 39 THAN ASN 87.  IT IS EXPECTED TO RESIDE ON THE     1YSC  86
FTNOTE   3 LATTER RESIDUE.                                              1YSC  87
HET    NAG    871      14     N-ACETYL-D-GLUCOSAMINE                    1YSC  88
HET    NAG   1681      14     N-ACETYL-D-GLUCOSAMINE                    1YSC  89
HET    NAG   3681      14     N-ACETYL-D-GLUCOSAMINE                    1YSC  90
FORMUL   2  NAG    3(C8 H15 N1 O6)                                      1YSC  91
FORMUL   3  HOH   *38(H2 O1)                                            1YSC  92
HELIX    1   A LEU     59  LEU     62  1                                1YSC  93
HELIX    2   B TRP     84  ASN     87  5                                1YSC  94
HELIX    3   C VAL    113  GLN    129  1                                1YSC  95
HELIX    4   D PRO    131  TYR    133  5                                1YSC  96
HELIX    5   E ALA    148  LEU    160  1                                1YSC  97
HELIX    6   F PRO    181  ALA    192  1                                1YSC  98
HELIX    7   G SER    204  SER    227  1                                1YSC  99
HELIX    8   H VAL    230  THR    251  1                                1YSC 100
HELIX    9   I THR    271  ASN    280  1                                1YSC 101
HELIX   10   J ASP    282  ALA    287  1                                1YSC 102
HELIX   11   K PHE    300  LEU    307  1                                1YSC 103
HELIX   12   L ASP    311  MET    313  5                                1YSC 104
HELIX   13   M HIS    317  ASN    325  1                                1YSC 105
HELIX   14   N TRP    343  THR    350  1                                1YSC 106
HELIX   15   O GLU    359  SER    363  1                                1YSC 107
HELIX   16   P VAL    399  ASP    402  1                                1YSC 108
HELIX   17   Q PRO    404  ILE    415  1                                1YSC 109
SHEET    1 S1A11 LYS     1  LYS     3  0                                1YSC 110
SHEET    2 S1A11 TYR    17  VAL    23 -1                                1YSC 111
SHEET    3 S1A11 LYS    28  PHE    35  1                                1YSC 112
SHEET    4 S1A11 THR    89  ILE    91 -1                                1YSC 113
SHEET    5 S1A11 VAL    46  LEU    50 -1                                1YSC 114
SHEET    6 S1A11 PHE   140  GLU   145 -1                                1YSC 115
SHEET    7 S1A11 LEU   169  GLY   175 -1                                1YSC 116
SHEET    8 S1A11 ILE   330  GLY   335 -1                                1YSC 117
SHEET    9 S1A11 PHE   387  VAL   392 -1                                1YSC 118
SHEET   10 S1A11 VAL   377  TYR   384  1                                1YSC 119
SHEET   11 S1A11 ARG   367  THR   370 -1                                1YSC 120
SHEET    1 S1B11 LYS     1  LYS     3  0                                1YSC 121
SHEET    2 S1B11 TYR    17  VAL    23 -1                                1YSC 122
SHEET    3 S1B11 LYS    28  PHE    35  1                                1YSC 123
SHEET    4 S1B11 TYR   103  SER   104 -1                                1YSC 124
SHEET    5 S1B11 VAL    46  LEU    50 -1                                1YSC 125
SHEET    6 S1B11 PHE   140  GLU   145 -1                                1YSC 126
SHEET    7 S1B11 LEU   169  GLY   175 -1                                1YSC 127
SHEET    8 S1B11 ILE   330  GLY   335 -1                                1YSC 128
SHEET    9 S1B11 PHE   387  VAL   392 -1                                1YSC 129
SHEET   10 S1B11 VAL   377  TYR   384  1                                1YSC 130
SHEET   11 S1B11 ARG   367  THR   370 -1                                1YSC 131
TURN     1  T1 GLU    24  ASP    27     HIGH BETA-LOOP                  1YSC 132
TURN     2  T2 GLY    52  GLY    55                                     1YSC 133
TURN     3  T3 GLY    72  LEU    75                                     1YSC 134
TURN     4  T4 ASN    85  ALA    88                                     1YSC 135
TURN     5  T5 PRO    96  VAL    99                                     1YSC 136
TURN     6  T6 VAL    99  SER   102                                     1YSC 137
TURN     7  T7 VAL   134  GLY   137                                     1YSC 138
TURN     8  T8 GLU   145  ALA   148                                     1YSC 139
TURN     9  T9 GLN   249  GLY   252                                     1YSC 140
TURN    10 T10 ASN   254  ASP   257     3.6 ANGSTROMS                   1YSC 141
SSBOND   1 CYS     56    CYS    298                                     1YSC 142
SSBOND   2 CYS    193    CYS    207                                     1YSC 143
SSBOND   3 CYS    217    CYS    240                                     1YSC 144
SSBOND   4 CYS    224    CYS    233                                     1YSC 145
SSBOND   5 CYS    262    CYS    268                                     1YSC 146
SITE     1 CAT  4 SER   146  ASP   338  HIS   397  GLU   145            1YSC 147
SITE     1 CBS  4 ASN    51  GLY    52  GLU   145  HIS   397            1YSC 148
SITE     1 S1P  7 THR    60  PHE    64  GLU    65  TYR   256            1YSC 149
SITE     2 S1P  7 TYR   269  LEU   272  MET   398                       1YSC 150
SITE     1 S1S  6 TYR   147  LEU   178  LEU   245  TRP   312            1YSC 151
SITE     2 S1S  6 ILE   340  CYS   341                                  1YSC 152
CRYST1  111.800  111.800  111.800  90.00  90.00  90.00 P 21 3       12  1YSC 153
ORIGX1      1.000000  0.000000  0.000000        0.00000                 1YSC 154
ORIGX2      0.000000  1.000000  0.000000        0.00000                 1YSC 155
ORIGX3      0.000000  0.000000  1.000000        0.00000                 1YSC 156
SCALE1      0.008945  0.000000  0.000000        0.00000                 1YSC 157
SCALE2      0.000000  0.008945  0.000000        0.00000                 1YSC 158
SCALE3      0.000000  0.000000  0.008945        0.00000                 1YSC 159

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Mail to: Nicolas Lenfant, Thierry Hotelier, Yves Bourne, Pascale Marchot and Arnaud Chatonnet.
Please cite: Lenfant 2013 Nucleic.Acids.Res. or Marchot Chatonnet 2012 Prot.Pept Lett.
For technical information about these pages see:
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