Structure of PDB 2bb0 Chain A Binding Site BS01

Receptor Information
>2bb0 Chain A (length=413) Species: 1423 (Bacillus subtilis) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
KQIDTILINIGQLLTMESSGPRAGKSMQDLHVIEDAVVGIHEQKIVFAGQ
KGAEAGYEADEIIDCSGRLVTPGLVDPHTHLVFGGSREKEMNLKLQGISY
LDILAQGGGILSTVKDTRAASEEELLQKAHFHLQRMLSYGTTTAEVKSGY
GLEKETELKQLRVAKKLHESQPVDLVSTFMGAHAIPPEYQNDPDDFLDQM
LSLLPEIKEQELASFADIFTETGVFTVSQSRRYLQKAAEAGFGLKIHADE
IDPLGGAELAGKLKAVSADHLVGTSDEGIKKLAEAGTIAVLLPGTTFYLG
KSTYARARAMIDEGVCVSLATDFNPGSSPTENIQLIMSIAALHLKMTAEE
IWHAVTVNAAYAIGKGEEAGQLKAGRSADLVIWQAPNYMYIPYHYGVNHV
HQVMKNGTIVVNR
Ligand information
Ligand IDACT
InChIInChI=1S/C2H4O2/c1-2(3)4/h1H3,(H,3,4)/p-1
InChIKeyQTBSBXVTEAMEQO-UHFFFAOYSA-M
SMILES
SoftwareSMILES
ACDLabs 10.04[O-]C(=O)C
OpenEye OEToolkits 1.5.0CC(=O)[O-]
CACTVS 3.341CC([O-])=O
FormulaC2 H3 O2
NameACETATE ION
ChEMBL
DrugBankDB14511
ZINC
PDB chain2bb0 Chain A Residue 1501 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB2bb0 A catalytic mechanism revealed by the crystal structures of the imidazolonepropionase from Bacillus subtilis
Resolution2.0 Å
Binding residue
(original residue number in PDB)		R89 Y102 I112 Y152 N326 G328
Binding residue
(residue number reindexed from 1)		R87 Y100 I110 Y150 N324 G326
Annotation score1
Enzymatic activity
Enzyme Commision number 3.5.2.7: imidazolonepropionase.
Gene Ontology
Molecular Function
GO:0005506 iron ion binding
GO:0008270 zinc ion binding
GO:0016787 hydrolase activity
GO:0016810 hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds
GO:0016812 hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in cyclic amides
GO:0046872 metal ion binding
GO:0050480 imidazolonepropionase activity
Biological Process
GO:0006547 L-histidine metabolic process
GO:0006548 L-histidine catabolic process
GO:0019556 L-histidine catabolic process to glutamate and formamide
GO:0019557 L-histidine catabolic process to glutamate and formate
Cellular Component
GO:0005737 cytoplasm

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:2bb0, PDBe:2bb0, PDBj:2bb0
PDBsum2bb0
PubMed16990261
UniProtP42084|HUTI_BACSU Imidazolonepropionase (Gene Name=hutI)

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