Structure of PDB 3kb6 Chain B

Receptor sequence
>3kb6B (length=334) Species: 63363 (Aquifex aeolicus) [Search protein sequence]
MNVLFTSVPQEDVPFYQEALKDLSLKIYTTDVSKVPENELKKAELISVFV
YDKLTEELLSKMPRLKLIHTRSVGFDHIDLDYCKKKGILVTHIPAYSPES
VAEHTFAMILTLVKRLKRIEDRVKKLNFSQDSEILARELNRLTLGVIGTG
RIGSRVAMYGLAFGMKVLCYDVVKREDLKEKGCVYTSLDELLKESDVISL
HVPYTKETHHMINEERISLMKDGVYLINTARGKVVDTDALYRAYQRGKFS
GLGLDVFEDEEILILKKYTEGKATDKNLKILELACKDNVIITPHIAYYTD
KSLERIREETVKVVKAFVKGDLEQIKGNFVVGPS
3D structure
PDB3kb6 Structure of D-lactate dehydrogenase from Aquifex aeolicus complexed with NAD(+) and lactic acid (or pyruvate).
ChainB
Resolution2.12 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) S97 R231 D255 E260 H294
Catalytic site (residue number reindexed from 1) S97 R231 D255 E260 H294
Enzyme Commision number 1.1.1.28: D-lactate 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 LAC B F49 S72 V73 G74 Y96 R231 H294 F49 S72 V73 G74 Y96 R231 H294
BS02 NAD B V73 Y96 V101 G150 R151 I152 D171 V172 P203 T229 A230 R231 H294 A296 Y297 V73 Y96 V101 G150 R151 I152 D171 V172 P203 T229 A230 R231 H294 A296 Y297
Gene Ontology
Molecular Function
GO:0000166 nucleotide binding
GO:0008720 D-lactate dehydrogenase activity
GO:0016491 oxidoreductase activity
GO:0016614 oxidoreductase activity, acting on CH-OH group of donors
GO:0016616 oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
GO:0051287 NAD binding

View graph for
Molecular Function
External links
PDB RCSB:3kb6, PDBe:3kb6, PDBj:3kb6
PDBsum3kb6
PubMed20054113
UniProtO66939

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