Structure of PDB 7cgq Chain C

Receptor sequence
>7cgqC (length=306) Species: 192 (Azospirillum brasilense) [Search protein sequence]
DQVSLGVVGIGKIARDQHLPAIDAEPGFKLTACASRHAEVTGVRNYRDLR
ALLAAERELDAVSLCAPPQVRYAQARAALEAGKHVMLEKPPGATLGEVAV
LEALARERGLTLFATWHSRCASAVEPAREWLATRAIRAVQVRWKADVRRW
HPGQQWIWEPGGLGVFDPGINALSIVTRILPRELVLREATLIVPSDVQTP
IAAELDCADTDGVPVRAEFDWRHGPVEQWEIAVDTADGVLAISRGGAQLS
IAGEPVELGPEREYPALYAHFHALIARGESDVDVRPLRLVADAFLFGRRV
QTDAFG
3D structure
PDB7cgq Crystal structure of bacterial L-arabinose 1-dehydrogenase in complex with L-arabinose and NADP+
ChainC
Resolution2.208 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 1.1.1.120: galactose 1-dehydrogenase (NADP(+)).
1.1.1.376: L-arabinose 1-dehydrogenase [NAD(P)(+)].
1.1.1.48: D-galactose 1-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 NAP C S37 R38 H39 P69 V72 S35 R36 H37 P67 V70
Gene Ontology
Molecular Function
GO:0000166 nucleotide binding
GO:0016491 oxidoreductase activity
GO:0016616 oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
GO:0019151 galactose 1-dehydrogenase activity
GO:0044103 L-arabinose 1-dehydrogenase (NADP+) activity
GO:0047910 galactose 1-dehydrogenase (NADP+) activity
GO:0050022 L-arabinose 1-dehydrogenase (NAD+) activity
GO:0070401 NADP+ binding
GO:0070403 NAD+ binding
Biological Process
GO:0019568 arabinose catabolic process
GO:0019570 L-arabinose catabolic process to 2-oxoglutarate
GO:0019572 L-arabinose catabolic process

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Molecular Function

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Biological Process
External links
PDB RCSB:7cgq, PDBe:7cgq, PDBj:7cgq
PDBsum7cgq
PubMed
UniProtQ53TZ2|ARAA_AZOBR L-arabinose 1-dehydrogenase (NAD(P)(+)) (Gene Name=araA)

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