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BioLiP

Structure of PDB 2dld Chain B

Receptor sequence
>2dldB (length=337) Species: 1587 (Lactobacillus helveticus) [Search protein sequence]
MTKVFAYAIRKDEEPFLNEWKEAHKDIDVDYTDKLLTPETAKLAKGADGV
VVYQQLDYTADTLQALADAGVTKMSLRNVGVDNIDMDKAKELGFQITNVP
VYSPNAIAEHAAIQAARVLRQDKRMDEKMAKRDLRWAPTIGREVRDQVVG
VVGTGHIGQVFMRIMEGFGAKVIAYDIFKNPELEKKGYYVDSLDDLYKQA
DVISLHVPDVPANVHMINDKSIAEMKDGVVIVNCSRGRLVDTDAVIRGLD
SGKIFGFVMDTYEDEVGVFNKDWEGKEFPDKRLADLIDRPNVLVTPHTAF
YTTHAVRNMVVKAFNNNLKLINGEKPDSPVALNKNKF
3D structure
PDB2dld Dehydrogenases Engineering to Correct Substrate Inhibition in a Commercial Dehydrogenase
ChainB
Resolution2.7 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) S103 R236 D260 E265 H297
Catalytic site (residue number reindexed from 1) S103 R236 D260 E265 H297
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 NAI B T154 G155 H156 I157 D176 I177 V207 P208 N213 C234 S235 R236 D260 H297 T154 G155 H156 I157 D176 I177 V207 P208 N213 C234 S235 R236 D260 H297
Gene Ontology
Molecular Function
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:2dld, PDBe:2dld, PDBj:2dld
PDBsum2dld
PubMed
UniProtP30901|LDHD_LACHE D-lactate dehydrogenase

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