Structure of PDB 5vlb Chain E

Receptor sequence
>5vlbE (length=433) Species: 3880 (Medicago truncatula) [Search protein sequence]
IKTYHLSNLTQTELLSLKSRPRIDFSSVFDIVNPIVDDVHAHGDAAVKQY
TSKFDKVDLENIVELVSDLPDPVLDPAIKEAFDVAYSNIYAFHAAQKSPE
KSVENMKGVQCKRVARSINSVGLYVPGGTAVLPSTALMLAVPAQIAGCKT
IVLANPPTRDGTTCKEVLYCAKKAGVTHLLKAGGAQAISAMAWGTETCPK
VEKIFGPGNQYVTAAKMILQNSEAMVSIDMPAGPSEVLVIADKHAIPSHV
AADLLSQAEHGPDSQVVLVIAGDGVDQNAIQEEVSKQCQSLPRGEFAAKA
LSHSFIVHARDMLEAITFSNMYAPEHLIINVKDAEKWESFIENAGSVFLG
SWTPESVGDYASGTNHVLPTYGYARMYSGVSLDSFLKYITVQSLTEEGLR
KLGPYVETMAEVEGLEAHKRAVTLRLQDIEARQ
3D structure
PDB5vlb Structures of Medicago truncatula L-Histidinol Dehydrogenase Show Rearrangements Required for NAD(+) Binding and the Cofactor Positioned to Accept a Hydride.
ChainE
Resolution2.25 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) Q299 H302 E367 H368 D401 H460
Catalytic site (residue number reindexed from 1) Q257 H260 E325 H326 D359 H418
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 E H302 D401 H260 D359
BS02 IMD E H302 D401 Y402 H408 H260 D359 Y360 H366
Gene Ontology
Molecular Function
GO:0000166 nucleotide binding
GO:0004399 histidinol dehydrogenase activity
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:0009507 chloroplast

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:5vlb, PDBe:5vlb, PDBj:5vlb
PDBsum5vlb
PubMed28874718
UniProtG7IKX3

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