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4AA8

Bovine chymosin at 1.8A resolution

Functional Information from GO Data
ChainGOidnamespacecontents
A0004190molecular_functionaspartic-type endopeptidase activity
A0006508biological_processproteolysis
Functional Information from PDB Data
site_idAC1
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CL A 1324
ChainResidue
ASER14
AGLN15
AGLU118

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CL A 1325
ChainResidue
AGLN150
AALA170
AILE171
AHOH2186
AHOH2243

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CL A 1326
ChainResidue
ASER129
AHOH2203
AHOH2268
APRO128

site_idAC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CL A 1327
ChainResidue
AASP151
AALA313
AHOH2114
AHOH2230

site_idAC5
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CL A 1328
ChainResidue
AASN264
AASN264
AHOH2260
AHOH2260

site_idAC6
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CL A 1329
ChainResidue
ALYS53
AARG57
ACYS211
AGLN212

site_idAC7
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CL A 1330
ChainResidue
ASER227
AGLN294
AHOH2303

site_idAC8
Number of Residues1
DetailsBINDING SITE FOR RESIDUE CL A 1331
ChainResidue
ASER273

Functional Information from PROSITE/UniProt
site_idPS00141
Number of Residues12
DetailsASP_PROTEASE Eukaryotic and viral aspartyl proteases active site. VLFDTGSSDFWV
ChainResidueDetails
AVAL31-VAL42
AALA213-GLY224

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues304
DetailsDomain: {"description":"Peptidase A1","evidences":[{"source":"PROSITE-ProRule","id":"PRU01103","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues2
DetailsActive site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU10094","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"329280","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"4612029","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

244693

PDB entries from 2025-11-12

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