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4A94

Structure of the carboxypeptidase inhibitor from Nerita versicolor in complex with human CPA4

Functional Information from GO Data
ChainGOidnamespacecontents
A0004181molecular_functionmetallocarboxypeptidase activity
A0006508biological_processproteolysis
A0008270molecular_functionzinc ion binding
B0004181molecular_functionmetallocarboxypeptidase activity
B0006508biological_processproteolysis
B0008270molecular_functionzinc ion binding
C0008191molecular_functionmetalloendopeptidase inhibitor activity
C0010951biological_processnegative regulation of endopeptidase activity
C0030414molecular_functionpeptidase inhibitor activity
C0046872molecular_functionmetal ion binding
D0008191molecular_functionmetalloendopeptidase inhibitor activity
D0010951biological_processnegative regulation of endopeptidase activity
D0030414molecular_functionpeptidase inhibitor activity
D0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 500
ChainResidue
AHIS69
AGLU72
AHIS196
DALA53

site_idAC2
Number of Residues8
DetailsBINDING SITE FOR RESIDUE NO3 A 1309
ChainResidue
ATYR248
AGLU270
DALA53
AHIS69
AARG127
AASN144
AARG145
AHIS196

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE NO3 A 1310
ChainResidue
AARG71
ALEU125
ATRP126
AARG127
ALYS128
AHOH2094

site_idAC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN B 501
ChainResidue
BHIS69
BGLU72
BHIS196
CALA53

site_idAC5
Number of Residues7
DetailsBINDING SITE FOR RESIDUE NO3 B 1309
ChainResidue
BHIS69
BARG127
BASN144
BARG145
BTYR248
BGLU270
CALA53

site_idAC6
Number of Residues8
DetailsBINDING SITE FOR RESIDUE NO3 B 1310
ChainResidue
BLEU125
BTRP126
BARG127
BLYS128
BGLU163
BHOH2035
BHOH2039
CGLN39

site_idAC7
Number of Residues6
DetailsBINDING SITE FOR RESIDUE NO3 C 1054
ChainResidue
BASN159
BCYS161
CARG7
CILE10
CPHE25
CHIS40

site_idAC8
Number of Residues7
DetailsBINDING SITE FOR RESIDUE NO3 D 1054
ChainResidue
AASN159
ACYS161
DARG7
DCYS9
DILE10
DPHE25
DHIS40

Functional Information from PROSITE/UniProt
site_idPS00132
Number of Residues23
DetailsCARBOXYPEPT_ZN_1 Zinc carboxypeptidases, zinc-binding region 1 signature. PaVwLnaGiHSrEwISQataiwT
ChainResidueDetails
APRO60-THR82

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 Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:22294694
ChainResidueDetails
CALA53
DALA53

site_idSWS_FT_FI2
Number of Residues12
DetailsBINDING: BINDING => ECO:0000269|PubMed:23746805, ECO:0007744|PDB:4BD9
ChainResidueDetails
AASN7
BSER13
BLYS85
BASP158
ATYR11
AHIS12
ASER13
ALYS85
AASP158
BASN7
BTYR11
BHIS12

site_idSWS_FT_FI3
Number of Residues6
DetailsBINDING: BINDING => ECO:0000269|PubMed:17506531, ECO:0007744|PDB:2PCU
ChainResidueDetails
AGLU15
APHE51
AARG84
BGLU15
BPHE51
BARG84

site_idSWS_FT_FI4
Number of Residues6
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU01379, ECO:0000269|PubMed:15738388, ECO:0000269|PubMed:16091843, ECO:0000269|PubMed:17506531, ECO:0000269|PubMed:22294694, ECO:0000269|PubMed:23746805, ECO:0007744|PDB:2BO9, ECO:0007744|PDB:2BOA, ECO:0007744|PDB:2PCU, ECO:0007744|PDB:4A94, ECO:0007744|PDB:4BD9
ChainResidueDetails
AHIS69
AGLU72
AHIS196
BHIS69
BGLU72
BHIS196

site_idSWS_FT_FI5
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:17506531, ECO:0000269|PubMed:23746805, ECO:0007744|PDB:2PCU, ECO:0007744|PDB:4BD9
ChainResidueDetails
ASER136
BSER136

site_idSWS_FT_FI6
Number of Residues2
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:15738388, ECO:0000269|PubMed:16091843, ECO:0000269|PubMed:17506531, ECO:0007744|PDB:2BO9, ECO:0007744|PDB:2BOA, ECO:0007744|PDB:2PCU
ChainResidueDetails
AASN148
BASN148

227344

PDB entries from 2024-11-13

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