Structure of PDB 1gpw Chain E

Receptor sequence
>1gpwE (length=251) Species: 2336 (Thermotoga maritima) [Search protein sequence]
MLAKRIIACLNVKDGRVVKNFENLRDSGDPVELGKFYSEIGIDELVFLDI
TASVEKRKTMLELVEKVAEQIDIPFTVGGGIHDFETASELILRGADKVSI
NTAAVENPSLITQIAQTFGSQAVVVAIDAKRVDGEFMVFTYSGKKNTGIL
LRDWVVEVEKRGAGEILLTSIDRDGTKSGYDTEMIRFVRPLTTLPIIASG
GAGKMEHFLEAFLAGADAALAASVFHFREIDVRELKEYLKKHGVNVRLEG
L
3D structure
PDB1gpw Structural Evidence for Ammonia Tunneling Across the (Beta Alpha)(8) Barrel of the Imidazole Glycerol Phosphate Synthase Bienzyme Complex.
ChainE
Resolution2.4 Å
3D
structure
Catalytic site residues are labeled in the structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]
Enzymatic activity
Catalytic site (original residue number in PDB) N11 D130
Catalytic site (residue number reindexed from 1) N11 D128
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 E G82 T104 G80 T102
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

View graph for
Molecular Function
View graph for
Biological Process
View graph for
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)

[Back to BioLiP]