Structure of PDB 4g07 Chain A

Receptor sequence
>4g07A (length=427) Species: 204722 (Brucella suis 1330) [Search protein sequence]
VTTLRQTDPDFEQKFAAFLSGDVDRAVREIVDRVRREGDSALLDYSRRFD
RIDLEKTGIAVTEAEIDAAFDAAPASTVEALKLARDRIEKHHARQLPKDD
RYTDALGVELGSRWTAIEAVGLYVPGGTASYPSSVLMNAMPAKVAGVDRI
VMVVPAPDGNLNPLVLVAARLAGVSEIYRVGGAQAIAALAYGTETIRPVA
KIVGPGNAYVAAAKRIVFGTVGIDMIAGPSEVLIVADKDNNPDWIAADLL
AQAEHDTAAQSILMTNDEAFAHAVEEAVERQLHTETASASWRDFGAVILV
KDFEDAIPLANRIAAEHLEIAVADAEAFVPRIRNAGSIFIGGYTPEVIGD
YVGGSNHVLPTARSARFSSGLSVLDYMKRTSLLKLGSEQLRALGPAAIEI
ARAEGLDAHAQSVAIRLNLLEHHHHHH
3D structure
PDB4g07 Structural basis for the rational design of new anti-Brucella agents: The crystal structure of the C366S mutant of l-histidinol dehydrogenase from Brucella suis.
ChainA
Resolution1.95 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) Q259 H262 E327 H328 D361 H420
Catalytic site (residue number reindexed from 1) Q252 H255 E316 H317 D350 H409
Enzyme Commision number 1.1.1.23: histidinol dehydrogenase.
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 ZN A E357 D361 E346 D350
BS02 ZN A D313 D316 D302 D305
Gene Ontology
Molecular Function
GO:0004399 histidinol dehydrogenase activity
GO:0008270 zinc ion binding
GO:0016491 oxidoreductase activity
GO:0016616 oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
GO:0046872 metal ion binding
GO:0051287 NAD binding
Biological Process
GO:0000105 L-histidine biosynthetic process
Cellular Component
GO:0005737 cytoplasm
GO:0005829 cytosol

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:4g07, PDBe:4g07, PDBj:4g07
PDBsum4g07
PubMed24140957
UniProtQ8G2R2|HISX_BRUSU Histidinol dehydrogenase (Gene Name=hisD)

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