Structure of PDB 7krm Chain A

Receptor sequence
>7krmA (length=240) Species: 470 (Acinetobacter baumannii) [Search protein sequence]
MLLQGKVALITGAASERGIGRATAEIFAQQGAKVIIVDLDLAQSQNAAKA
LGEGHMGLAANVANEEQVKAAVEQALQHYGKIDILINNAGITQPIKTLDI
QRSDYDRVLDVSLRGTLIMSQAVIPSMKANGGGSIVCLSSVSAQRGGGIF
GGPHYSAAKAGVLGLAKAMAREFGGDQIRVNSLTPGLIQDDRRHDILAGI
PLGRLGKAQDVANAALFLASDLSAYLTGVTLDVNGGMLIH
3D structure
PDB7krm Putative FabG bound to NADH from Acinetobacter baumannii
ChainA
Resolution1.9 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) G18 S140 Y155
Catalytic site (residue number reindexed from 1) G18 S140 Y155
Enzyme Commision number 1.1.1.47: glucose 1-dehydrogenase [NAD(P)(+)].
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 NAD A G12 S15 G18 I19 D38 L39 A60 N61 V62 N88 V111 S139 S140 Y155 K159 P185 I188 G12 S15 G18 I19 D38 L39 A60 N61 V62 N88 V111 S139 S140 Y155 K159 P185 I188
Gene Ontology
Molecular Function
GO:0000166 nucleotide binding
GO:0004316 3-oxoacyl-[acyl-carrier-protein] reductase (NADPH) activity
GO:0016491 oxidoreductase activity
GO:0016616 oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
GO:0047936 glucose 1-dehydrogenase [NAD(P)+] activity
Biological Process
GO:0030497 fatty acid elongation

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Molecular Function
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Biological Process
External links
PDB RCSB:7krm, PDBe:7krm, PDBj:7krm
PDBsum7krm
PubMed
UniProtA0A077GFB1

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