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4UEZ

Crystal structure of the human CARBOXYPEPTIDASE A1 in complex with the PHOSPHINIC INHIBITOR Acetyl-Leu-Phe-Y(PO2CH2)-Phe-OH

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 Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 420
ChainResidue
AHIS179
AGLU182
AHIS306
ALFF421

site_idAC2
Number of Residues23
DetailsBINDING SITE FOR RESIDUE LFF A 421
ChainResidue
AARG255
AGLU273
AHIS306
ASER307
ATYR308
ASER309
AILE353
AILE357
ATYR358
AALA360
ASER363
ATHR378
AGLU380
APHE389
AZN420
AHOH2045
BGLU273
BLFF421
AHIS179
AARG181
AGLU182
AARG237
AASN254

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN B 420
ChainResidue
BHIS179
BGLU182
BHIS306
BLFF421

site_idAC4
Number of Residues23
DetailsBINDING SITE FOR RESIDUE LFF B 421
ChainResidue
AGLU273
ALFF421
BHIS179
BARG181
BGLU182
BARG237
BASN254
BARG255
BTHR274
BHIS306
BSER307
BTYR308
BSER309
BILE353
BILE357
BTYR358
BALA360
BSER363
BTHR378
BGLU380
BPHE389
BZN420
BHOH2047

Functional Information from PROSITE/UniProt
site_idPS00132
Number of Residues23
DetailsCARBOXYPEPT_ZN_1 Zinc carboxypeptidases, zinc-binding region 1 signature. PaIwIdtGiHSrEwVTQasgvwF
ChainResidueDetails
APRO170-PHE192

site_idPS00133
Number of Residues11
DetailsCARBOXYPEPT_ZN_2 Zinc carboxypeptidases, zinc-binding region 2 signature. HSYSQLLmYPY
ChainResidueDetails
AHIS306-TYR316

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Proton donor/acceptor => ECO:0000255|PROSITE-ProRule:PRU01379
ChainResidueDetails
AGLU380
BGLU380

site_idSWS_FT_FI2
Number of Residues6
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU01379, ECO:0000269|PubMed:18566513, ECO:0007744|PDB:2V77
ChainResidueDetails
AHIS179
AGLU182
AHIS306
BHIS179
BGLU182
BHIS306

site_idSWS_FT_FI3
Number of Residues8
DetailsBINDING: BINDING => ECO:0000269|PubMed:18566513, ECO:0007744|PDB:2V77
ChainResidueDetails
AARG237
AASN254
ASER307
ATYR358
BARG237
BASN254
BSER307
BTYR358

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PDB entries from 2024-07-31

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