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1OBR

CARBOXYPEPTIDASE T

Functional Information from GO Data
ChainGOidnamespacecontents
A0004181molecular_functionmetallocarboxypeptidase activity
A0006508biological_processproteolysis
A0008270molecular_functionzinc ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 400
ChainResidue
AHIS69
AGLU72
AHIS204
AHOH414

site_idAC2
Number of Residues7
DetailsBINDING SITE FOR RESIDUE CA A 401
ChainResidue
AHOH472
AHOH481
AASP56
AGLU57
AGLU61
AGLU104
AARG189

site_idAC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CA A 402
ChainResidue
ASER50
AASP51
AGLU57
AGLU59
AHOH426

site_idAC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CA A 403
ChainResidue
AASP51
AGLU59
AASN101
AHOH516

site_idAC5
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CA A 404
ChainResidue
ASER7
ATYR9
AGLU14
AHOH455
AHOH466

site_idAC6
Number of Residues6
DetailsBINDING SITE FOR RESIDUE SO4 A 405
ChainResidue
AHIS69
AARG129
AASN146
AARG147
ATYR255
AGLU277

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

site_idPS00133
Number of Residues11
DetailsCARBOXYPEPT_ZN_2 Zinc carboxypeptidases, zinc-binding region 2 signature. HTYSELIlYPY
ChainResidueDetails
AHIS204-TYR214

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Proton donor/acceptor => ECO:0000255|PROSITE-ProRule:PRU01379, ECO:0000305|PubMed:1521526
ChainResidueDetails
AGLU277

site_idSWS_FT_FI2
Number of Residues3
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU01379, ECO:0000269|PubMed:1521526
ChainResidueDetails
AHIS69
AGLU72
AHIS204

218853

PDB entries from 2024-04-24

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