Loading
PDBj
MenuPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDBDonate
RCSB PDBPDBeBMRBAdv. SearchSearch help

1KA2

Structure of Pyrococcus furiosus Carboxypeptidase Apo-Mg

Functional Information from GO Data
ChainGOidnamespacecontents
A0004180molecular_functioncarboxypeptidase activity
A0004181molecular_functionmetallocarboxypeptidase activity
A0006508biological_processproteolysis
A0008233molecular_functionpeptidase activity
A0008237molecular_functionmetallopeptidase activity
A0016787molecular_functionhydrolase activity
A0046872molecular_functionmetal ion binding
A0046914molecular_functiontransition metal 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 Residues493
DetailsDomain: {"description":"Peptidase M32","evidences":[{"source":"PROSITE-ProRule","id":"PRU01378","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues2
DetailsMotif: {"description":"HPF","evidences":[{"source":"PROSITE-ProRule","id":"PRU01378","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues4
DetailsMotif: {"description":"DXRXT","evidences":[{"source":"PROSITE-ProRule","id":"PRU01378","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues4
DetailsMotif: {"description":"HEXXH","evidences":[{"source":"PROSITE-ProRule","id":"PRU01378","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues3
DetailsMotif: {"description":"HES/GQ","evidences":[{"source":"PROSITE-ProRule","id":"PRU01378","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues5
DetailsMotif: {"description":"I/NRXXA/SD","evidences":[{"source":"PROSITE-ProRule","id":"PRU01378","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues7
DetailsMotif: {"description":"GXXQDXHW","evidences":[{"source":"PROSITE-ProRule","id":"PRU01378","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI8
Number of Residues1
DetailsActive site: {"description":"Proton donor/acceptor","evidences":[{"source":"PROSITE-ProRule","id":"PRU01378","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI9
Number of Residues3
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"11839307","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

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

246031

PDB entries from 2025-12-10

PDB statisticsPDBj update infoContact PDBjnumon