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4PEP

THE MOLECULAR AND CRYSTAL STRUCTURES OF MONOCLINIC PORCINE PEPSIN REFINED AT 1.8 ANGSTROMS RESOLUTION

Replaces:  1PEP
Functional Information from GO Data
ChainGOidnamespacecontents
A0004190molecular_functionaspartic-type endopeptidase activity
A0006508biological_processproteolysis
Functional Information from PROSITE/UniProt
site_idPS00141
Number of Residues12
DetailsASP_PROTEASE Eukaryotic and viral aspartyl proteases active site. VIFDTGSSNLWV
ChainResidueDetails
AVAL29-VAL40
AALA212-GLY223

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: ACT_SITE => ECO:0000255|PROSITE-ProRule:PRU10094, ECO:0000269|PubMed:1097438, ECO:0000269|PubMed:4897201
ChainResidueDetails
AASP32
AASP215

site_idSWS_FT_FI2
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P03954
ChainResidueDetails
ASEP68

Catalytic Information from CSA
site_idCSA1
Number of Residues1
DetailsAnnotated By Reference To The Literature 1am5
ChainResidueDetails
AASP32

site_idCSA2
Number of Residues1
DetailsAnnotated By Reference To The Literature 1am5
ChainResidueDetails
AASP215

site_idCSA3
Number of Residues4
DetailsAnnotated By Reference To The Literature 1am5
ChainResidueDetails
AASP215
ASER35
ATHR218
AASP32

site_idCSA4
Number of Residues4
DetailsAnnotated By Reference To The Literature 1am5
ChainResidueDetails
AASP215
ATHR216
AASP32
ATHR33

site_idCSA5
Number of Residues3
DetailsAnnotated By Reference To The Literature 1am5
ChainResidueDetails
AASP215
ASER35
AASP32

site_idCSA6
Number of Residues4
DetailsAnnotated By Reference To The Literature 1am5
ChainResidueDetails
AASP215
ATYR75
ASER35
AASP32

site_idCSA7
Number of Residues4
DetailsAnnotated By Reference To The Literature 1am5
ChainResidueDetails
AASP215
ATHR218
AASP32
ATHR33

224931

PDB entries from 2024-09-11

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