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2V77

Crystal Structure of Human Carboxypeptidase A1

Functional Information from GO Data
ChainGOidnamespacecontents
A0004181molecular_functionmetallocarboxypeptidase activity
A0006508biological_processproteolysis
A0008270molecular_functionzinc ion binding
B0004181molecular_functionmetallocarboxypeptidase activity
B0006508biological_processproteolysis
B0008270molecular_functionzinc ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues16
DetailsBINDING SITE FOR RESIDUE PAY A 400
ChainResidue
AHIS69
AMET203
ATYR248
ATHR268
AGLU270
APHE279
AZN1042
AHOH2365
AARG71
AGLU72
AARG127
AASN144
AARG145
AHIS196
ASER197
ATYR198

site_idAC2
Number of Residues16
DetailsBINDING SITE FOR RESIDUE PAY B 400
ChainResidue
BHIS69
BARG71
BGLU72
BARG127
BASN144
BARG145
BHIS196
BSER197
BTYR198
BMET203
BTYR248
BTHR268
BGLU270
BPHE279
BZN1042
BHOH2399

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A1042
ChainResidue
AHIS69
AGLU72
AHIS196
APAY400

site_idAC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN B1042
ChainResidue
BHIS69
BGLU72
BHIS196
BPAY400

site_idAC5
Number of Residues8
DetailsBINDING SITE FOR RESIDUE EPE A1309
ChainResidue
ATRP126
AARG130
ALEU137
ACYS138
AILE139
AHOH2370
BTHR274
BARG276

site_idAC6
Number of Residues5
DetailsBINDING SITE FOR RESIDUE EPE B1309
ChainResidue
AARG276
BTRP126
BARG130
BLEU137
BILE139

site_idAC7
Number of Residues6
DetailsBINDING SITE FOR RESIDUE EPE A1310
ChainResidue
ALYS51
ASER57
ALYS58
APHE106
APHE182
AASP185

Functional Information from PROSITE/UniProt
site_idPS00132
Number of Residues23
DetailsCARBOXYPEPT_ZN_1 Zinc carboxypeptidases, zinc-binding region 1 signature. PaIwIdtGiHSrEwVTQasgvwF
ChainResidueDetails
APRO60-PHE82

site_idPS00133
Number of Residues11
DetailsCARBOXYPEPT_ZN_2 Zinc carboxypeptidases, zinc-binding region 2 signature. HSYSQLLmYPY
ChainResidueDetails
AHIS196-TYR206

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues586
DetailsDomain: {"description":"Peptidase M14","evidences":[{"source":"PROSITE-ProRule","id":"PRU01379","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues2
DetailsActive site: {"description":"Proton donor/acceptor","evidences":[{"source":"PROSITE-ProRule","id":"PRU01379","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues14
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"18566513","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2V77","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues6
DetailsBinding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU01379","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"18566513","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2V77","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 1cbx
ChainResidueDetails
AARG127
AGLU270

site_idCSA2
Number of Residues2
DetailsAnnotated By Reference To The Literature 1cbx
ChainResidueDetails
BARG127
BGLU270

site_idCSA3
Number of Residues3
DetailsAnnotated By Reference To The Literature 1cbx
ChainResidueDetails
AARG71
AGLU270
AARG127

site_idCSA4
Number of Residues3
DetailsAnnotated By Reference To The Literature 1cbx
ChainResidueDetails
BARG71
BGLU270
BARG127

239149

PDB entries from 2025-07-23

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