Structure of PDB 1kah Chain B

Receptor sequence

>1kahB (length=434) Species: 562 (Escherichia coli)

MSFNTIIDWNSCTAEQQRQLLMRPAISASESITRTVNDILDNVKARGDEA
LREYSAKFDKTTVTALKVSAEEIAAASERLSDELKQAMAVAVKNIETFHT
AQKLPPVDVETQPGVRCQQVTRPVASVGLYIPGGSAPLFSTVLMLATPAS
IAGCKKVVLCSPPPIADEILYAAQLCGVQDVFNVGGAQAIAALAFGTESV
PKVDKIFGPGNAFVTEAKRQVSQRLDGAAIDMPAGPSEVLVIADSGATPD
FVASDLLSQAEHGPDSQVILLTPAADMARRVAEAVERQLAELPRAETARQ
ALNASRLIVTKDLAQCVEISNQYGPEHLIIQTRNARELVDSITSAGSVFL
GDWSPESAGDYASGTNHVLPTYGYTATCSSLGLADFQKRMTVQELSKEGF
SALASTIETLAAAERLTAHKNAVTLRVNALKEQA

3D structure

• PDB: 1kah Mechanism of action and NAD+-binding mode revealed by the crystal structure of L-histidinol dehydrogenase.
• Chain: B
• Resolution: 2.1 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): Q259 H262 E326 H327 D360 H419
• Catalytic site (residue number reindexed from 1): Q259 H262 E326 H327 D360 H419
• 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	HIS	B	H262 D360 Y361 H367	H262 D360 Y361 H367
BS02	ZN	B	H262 D360	H262 D360

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

External links

• PDB: RCSB:1kah, PDBe:1kah, PDBj:1kah
• PDBsum: 1kah
• PubMed: 11842181
• UniProt: P06988|HISX_ECOLI Histidinol dehydrogenase (Gene Name=hisD)