Structure of PDB 5vld Chain F

Receptor sequence
>5vldF (length=435) Species: 3880 (Medicago truncatula) [Search protein sequence]
PIKTYHLSNLTQTELLSLKSRPRIDFSSVFDIVNPIVDDVHAHGDAAVKQ
YTSKFDKVDLENIVELVSDLPDPVLDPAIKEAFDVAYSNIYAFHAAQKSP
EKSVENMKGVQCKRVARSINSVGLYVPGGTAVLPSTALMLAVPAQIAGCK
TIVLANPPTRDGTTCKEVLYCAKKAGVTHLLKAGGAQAISAMAWGTETCP
KVEKIFGPGNQYVTAAKMILQNSEAMVSIDMPAGPSEVLVIADKHAIPSH
VAADLLSQAEHGPDSQVVLVIAGDGVDQNAIQEEVSKQCQSLPRGEFAAK
ALSHSFIVHARDMLEAITFSNMYAPEHLIINVKDAEKWESFIENAGSVFL
GSWTPESVGDYASGTNHVLPTYGYARMYSGVSLDSFLKYITVQSLTEEGL
RKLGPYVETMAEVEGLEAHKRAVTLRLQDIEARQV
3D structure
PDB5vld Structures of Medicago truncatula L-Histidinol Dehydrogenase Show Rearrangements Required for NAD(+) Binding and the Cofactor Positioned to Accept a Hydride.
ChainF
Resolution2.59 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) Q258 H261 E326 H327 D360 H419
Enzyme Commision number 1.1.1.23: histidinol dehydrogenase.
Interaction with ligand
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:5vld, PDBe:5vld, PDBj:5vld
PDBsum5vld
PubMed28874718
UniProtG7IKX3

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