Structure of PDB 2wjz Chain A Binding Site BS01
Receptor Information
>2wjz Chain A (length=251) Species:
2336
(Thermotoga maritima) [
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MLAKRIIACLDVKDGRVVKGTNFENLRDSGDPVELGKFYSEIGIDELVFL
DITASVEKRKTMLELVEKVAEQIDIPFTVGGGIHDFETASELILRGADKV
SINTAAVENPSLITQIAQTFGSQAVVVAIDAKRVDGEFMVFTYSGKKNTG
ILLRDWVVEVEKRGAGEILLTSIDRDGTKSGYDTEMIRFVRPLTTLPIIA
SGGAGKMEHFLEAFLAGADAALAASVFHFREIDVRELKEYLKKHGVNVRL
E
Ligand information
Ligand ID
PO4
InChI
InChI=1S/H3O4P/c1-5(2,3)4/h(H3,1,2,3,4)/p-3
InChIKey
NBIIXXVUZAFLBC-UHFFFAOYSA-K
SMILES
Software
SMILES
CACTVS 3.341
[O-][P]([O-])([O-])=O
ACDLabs 10.04
[O-]P([O-])([O-])=O
OpenEye OEToolkits 1.5.0
[O-]P(=O)([O-])[O-]
Formula
O4 P
Name
PHOSPHATE ION
ChEMBL
DrugBank
DB14523
ZINC
PDB chain
2wjz Chain A Residue 1252 [
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Receptor-Ligand Complex Structure
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PDB
2wjz
Catalysis Uncoupling in a Glutamine Amidotransferase Bienzyme by Unblocking the Glutaminase Active Site.
Resolution
2.601 Å
Binding residue
(original residue number in PDB)
G82 N103 T104
Binding residue
(residue number reindexed from 1)
G82 N103 T104
Annotation score
1
Enzymatic activity
Catalytic site (original residue number in PDB)
D11 D130
Catalytic site (residue number reindexed from 1)
D11 D130
Enzyme Commision number
4.3.2.10
: imidazole glycerol-phosphate synthase.
Gene Ontology
Molecular Function
GO:0000107
imidazoleglycerol-phosphate synthase activity
GO:0005515
protein binding
GO:0016829
lyase activity
Biological Process
GO:0000105
L-histidine biosynthetic process
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:2wjz
,
PDBe:2wjz
,
PDBj:2wjz
PDBsum
2wjz
PubMed
23261602
UniProt
Q9X0C6
|HIS6_THEMA Imidazole glycerol phosphate synthase subunit HisF (Gene Name=hisF)
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