Structure of PDB 1gpw Chain C

Receptor sequence
>1gpwC (length=253) Species: 2336 (Thermotoga maritima) [Search protein sequence]
MLAKRIIACLNVKDGRVVKGTNFENLRDSGDPVELGKFYSEIGIDELVFL
DITASVEKRKTMLELVEKVAEQIDIPFTVGGGIHDFETASELILRGADKV
SINTAAVENPSLITQIAQTFGSQAVVVAIDAKRVDGEFMVFTYSGKKNTG
ILLRDWVVEVEKRGAGEILLTSIDRDGTKSGYDTEMIRFVRPLTTLPIIA
SGGAGKMEHFLEAFLAGADAALAASVFHFREIDVRELKEYLKKHGVNVRL
EGL
3D structure
PDB1gpw Structural Evidence for Ammonia Tunneling Across the (Beta Alpha)(8) Barrel of the Imidazole Glycerol Phosphate Synthase Bienzyme Complex.
ChainC
Resolution2.4 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) N11 D130
Catalytic site (residue number reindexed from 1) N11 D130
Enzyme Commision number 4.3.2.10: imidazole glycerol-phosphate synthase.
Interaction with ligand
Site
#		 Ligand Ligand
chain		 Binding residues on receptor
(original residue number in PDB)		 Binding residues on receptor
(residue number reindexed from 1)		 Binding affinity
BS01 PO4 C D176 G177 S225 D176 G177 S225
BS02 PO4 C G82 N103 T104 G82 N103 T104
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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Cellular Component
External links
PDB RCSB:1gpw, PDBe:1gpw, PDBj:1gpw
PDBsum1gpw
PubMed11839304
UniProtQ9X0C6|HIS6_THEMA Imidazole glycerol phosphate synthase subunit HisF (Gene Name=hisF)

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