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

2BB0

Structure of Imidazolonepropionase from Bacillus subtilis

Functional Information from GO Data
ChainGOidnamespacecontents
A0005506molecular_functioniron ion binding
A0005737cellular_componentcytoplasm
A0006547biological_processL-histidine metabolic process
A0006548biological_processL-histidine catabolic process
A0008270molecular_functionzinc ion binding
A0016787molecular_functionhydrolase activity
A0016810molecular_functionhydrolase activity, acting on carbon-nitrogen (but not peptide) bonds
A0016812molecular_functionhydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in cyclic amides
A0019556biological_processL-histidine catabolic process to glutamate and formamide
A0019557biological_processL-histidine catabolic process to glutamate and formate
A0046872molecular_functionmetal ion binding
A0050480molecular_functionimidazolonepropionase activity
B0005506molecular_functioniron ion binding
B0005737cellular_componentcytoplasm
B0006547biological_processL-histidine metabolic process
B0006548biological_processL-histidine catabolic process
B0008270molecular_functionzinc ion binding
B0016787molecular_functionhydrolase activity
B0016810molecular_functionhydrolase activity, acting on carbon-nitrogen (but not peptide) bonds
B0016812molecular_functionhydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in cyclic amides
B0019556biological_processL-histidine catabolic process to glutamate and formamide
B0019557biological_processL-histidine catabolic process to glutamate and formate
B0046872molecular_functionmetal ion binding
B0050480molecular_functionimidazolonepropionase activity
Functional Information from PDB Data
site_idAC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE ACT A 1501
ChainResidue
AARG89
ATYR102
AILE112
ATYR152
AASN326
AGLY328

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE ACT B 2501
ChainResidue
BTYR152
BASN326
BGLY328
BARG89
BTYR102
BILE112

site_idAC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE ZN A 1601
ChainResidue
AHIS80
AHIS82
AHIS249
AASP324
AHOH1729

site_idAC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE ZN B 2601
ChainResidue
BHIS80
BHIS82
BHIS249
BASP324
BHOH2714

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues8
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"16990261","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2BB0","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2G3F","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues6
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"16990261","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"2G3F","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues8
DetailsBinding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00372","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

239492

PDB entries from 2025-07-30

PDB statisticsPDBj update infoContact PDBjnumon