Structure of PDB 3cq5 Chain B

Receptor sequence
>3cq5B (length=366) Species: 196627 (Corynebacterium glutamicum ATCC 13032) [Search protein sequence]
MTKITLSDLPLREELRGEHAYGAPQLNVDIRLNTNENPYPPSEALVADLV
ATVDKIATELNRYPERDAVELRDELAAYITKQTGVAVTRDNLWAANGSNE
ILQQLLQAFGGPGRTALGFQPSYSMHPILAKGTHTEFIAVSRGADFRIDM
DVALEEIRAKQPDIVFVTTPNNPTGDVTSLDDVERIINVAPGIVIVDEAY
AEFSPSPSATTLLEKYPTKLVVSRTMSKAFDFAGGRLGYFVANPAFIDAV
MLVRLPYHLSALSQAAAIVALRHSADTLGTVEKLSVERVRVAARLEELGY
AVVPSESNFVFFGDFSDQHAAWQAFLDRGVLIRDVGIAGHLRTTIGVPEE
NDAFLDAAAEIIKLNL
3D structure
PDB3cq5 Insights into the structural basis of substrate recognition by histidinol-phosphate aminotransferase from Corynebacterium glutamicum
ChainB
Resolution1.8 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 2.6.1.9: histidinol-phosphate transaminase.
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 PMP B G97 S98 N99 Y123 N172 D197 A199 Y200 T225 S227 K228 R236 G97 S98 N99 Y123 N172 D197 A199 Y200 T225 S227 K228 R236
Gene Ontology
Molecular Function
GO:0004400 histidinol-phosphate transaminase activity
GO:0008483 transaminase activity
GO:0030170 pyridoxal phosphate binding
Biological Process
GO:0000105 L-histidine biosynthetic process
GO:0009058 biosynthetic process

View graph for
Molecular Function
View graph for
Biological Process
External links
PDB RCSB:3cq5, PDBe:3cq5, PDBj:3cq5
PDBsum3cq5
PubMed18560156
UniProtQ9KJU4|HIS8_CORGL Histidinol-phosphate aminotransferase (Gene Name=hisC)

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