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6SN6

CARBOXYPEPTIDASE T WITH N-SULFAMOYL-L-GLUTAMIC ACID

Replaces:  5MYH
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 401
ChainResidue
AHIS69
AGLU72
AHIS204
A3K0402

site_idAC2
Number of Residues14
Detailsbinding site for residue 3K0 A 402
ChainResidue
AHIS204
ATHR205
AALA251
ATYR255
ATHR257
AASP260
AGLU277
AZN401
AHOH661
AHIS69
AGLU72
AARG129
AASN146
AARG147

site_idAC3
Number of Residues6
Detailsbinding site for residue CA A 403
ChainResidue
ASER7
ATYR9
AGLU14
AHOH657
AHOH673
AHOH752

site_idAC4
Number of Residues5
Detailsbinding site for residue CA A 404
ChainResidue
ASER50
AASP51
AGLU57
AGLU59
AHOH592

site_idAC5
Number of Residues6
Detailsbinding site for residue CA A 405
ChainResidue
AASP56
AGLU57
AGLU61
AGLU104
AHOH519
AHOH650

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

224572

PDB entries from 2024-09-04

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