Structure of PDB 1kar Chain A

Receptor sequence
>1karA (length=431) Species: 562 (Escherichia coli) [Search protein sequence]
NTIIDWNSCTAEQQRQLLMRPAISASESITRTVNDILDNVKARGDEALRE
YSAKFDKTTVTALKVSAEEIAAASERLSDELKQAMAVAVKNIETFHTAQK
LPPVDVETQPGVRCQQVTRPVASVGLYIPGGSAPLFSTVLMLATPASIAG
CKKVVLCSPPPIADEILYAAQLCGVQDVFNVGGAQAIAALAFGTESVPKV
DKIFGPGNAFVTEAKRQVSQRLDGAAIDMPAGPSEVLVIADSGATPDFVA
SDLLSQAEHGPDSQVILLTPAADMARRVAEAVERQLAELPRAETARQALN
ASRLIVTKDLAQCVEISNQYGPEHLIIQTRNARELVDSITSAGSVFLGDW
SPESAGDYASGTNHVLPTYGYTATCSSLGLADFQKRMTVQELSKEGFSAL
ASTIETLAAAERLTAHKNAVTLRVNALKEQA
3D structure
PDB1kar Mechanism of action and NAD+-binding mode revealed by the crystal structure of L-histidinol dehydrogenase.
ChainA
Resolution2.1 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 E326 H327 D360 H419
Catalytic site (residue number reindexed from 1) Q256 H259 E323 H324 D357 H416
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 H262 D360 H259 D357
BS02 HSM A S140 H262 D360 Y361 H367 S137 H259 D357 Y358 H364
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:0030145 manganese ion binding
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:1kar, PDBe:1kar, PDBj:1kar
PDBsum1kar
PubMed11842181
UniProtP06988|HISX_ECOLI Histidinol dehydrogenase (Gene Name=hisD)

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