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1KA2

Structure of Pyrococcus furiosus Carboxypeptidase Apo-Mg

Functional Information from GO Data
ChainGOidnamespacecontents
A0004180molecular_functioncarboxypeptidase activity
A0004181molecular_functionmetallocarboxypeptidase activity
A0006508biological_processproteolysis
A0008237molecular_functionmetallopeptidase activity
A0046872molecular_functionmetal ion binding
A0050897molecular_functioncobalt ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MG A 501
ChainResidue
AHIS269
AHIS273
AGLU299
AHOH502
AHOH518
AHOH537

Functional Information from PROSITE/UniProt
site_idPS00142
Number of Residues10
DetailsZINC_PROTEASE Neutral zinc metallopeptidases, zinc-binding region signature. STVHEFGHAL
ChainResidueDetails
ASER266-LEU275

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Proton donor/acceptor => ECO:0000255|PROSITE-ProRule:PRU01378
ChainResidueDetails
AGLU270

site_idSWS_FT_FI2
Number of Residues3
DetailsBINDING: BINDING => ECO:0000269|PubMed:11839307
ChainResidueDetails
AHIS269
AHIS273
AGLU299

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 1i1i
ChainResidueDetails
ATYR423
AGLU299

229380

PDB entries from 2024-12-25

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