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1CPB

STRUCTURE OF CARBOXYPEPTIDASE B AT 2.8 ANGSTROMS RESOLUTION

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

site_idPS00133
Number of Residues11
DetailsCARBOXYPEPT_ZN_2 Zinc carboxypeptidases, zinc-binding region 2 signature. HSYSQMMlYPY
ChainResidueDetails
BHIS196-TYR206

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues3
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU01379
ChainResidueDetails
BVAL179
BPHE182
BGLU306

site_idSWS_FT_FI2
Number of Residues3
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:P00730
ChainResidueDetails
BTHR236
BGLY253
BHIS307

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 1cbx
ChainResidueDetails
BARG127
BGLU270

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PDB entries from 2024-10-09

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