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3GLJ

A polymorph of carboxypeptidase B zymogen structure

Functional Information from GO Data
ChainGOidnamespacecontents
A0004180molecular_functioncarboxypeptidase activity
A0004181molecular_functionmetallocarboxypeptidase activity
A0005576cellular_componentextracellular region
A0005615cellular_componentextracellular space
A0006508biological_processproteolysis
A0008237molecular_functionmetallopeptidase activity
A0008270molecular_functionzinc ion binding
A0031410cellular_componentcytoplasmic vesicle
A0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 401
ChainResidue
AHIS69
AGLU72
AHIS196
AHOH315

site_idAC2
Number of Residues8
DetailsBINDING SITE FOR RESIDUE GOL A 309
ChainResidue
AILE263
AHOH366
AHOH507
ALEU187
ASER188
AILE189
ALYS190
AGLY262

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE GOL A 310
ChainResidue
AHIS7
ATYR9
AGLN24
AHIS27
AGLU28
ASER31

site_idAC4
Number of Residues10
DetailsBINDING SITE FOR RESIDUE GOL A 311
ChainResidue
ASER27
AGLU28
APRO30
ACYS152
ATHR153
ATHR154
AGLY155
AALA156
ATHR158
AHOH463

site_idAC5
Number of Residues8
DetailsBINDING SITE FOR RESIDUE GOL A 312
ChainResidue
ALEU32
AILE33
ASER34
ALYS51
AGLY53
APRO55
AHOH523
AHOH582

site_idAC6
Number of Residues4
DetailsBINDING SITE FOR RESIDUE GOL A 313
ChainResidue
ATYR299
AASN302
ATYR303
AHOH571

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

site_idPS00133
Number of Residues11
DetailsCARBOXYPEPT_ZN_2 Zinc carboxypeptidases, zinc-binding region 2 signature. HSYSQMIlYPY
ChainResidueDetails
AHIS196-TYR206

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Proton donor/acceptor => ECO:0000255|PROSITE-ProRule:PRU01379
ChainResidueDetails
AGLU270

site_idSWS_FT_FI2
Number of Residues3
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU01379
ChainResidueDetails
AHIS69
AGLU72
AHIS196

site_idSWS_FT_FI3
Number of Residues4
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:P00730
ChainResidueDetails
AARG127
AASN144
ASER197
ATYR248

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 1cbx
ChainResidueDetails
AARG127
AGLU270

site_idCSA2
Number of Residues3
DetailsAnnotated By Reference To The Literature 1cbx
ChainResidueDetails
AARG71
AGLU270
AARG127

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PDB entries from 2024-10-30

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