Structure of PDB 1j49 Chain A

Receptor sequence
>1j49A (length=332) Species: 1585 (Lactobacillus delbrueckii subsp. bulgaricus) [Search protein sequence]
MTKIFAYAIREDEKPFLKEWEDAHKDVEVEYTDKLLTPETVALAKGADGV
VVYQQLDYIAETLQALADNGITKMSLRNVGVDNIDMAKAKELGFQITNVP
VYSPNAIAEHAAIQAARILRQDKAMDEKVARHDLRWAPTIGREVRDQVVG
VVGTGHIGQVFMQIMEGFGAKVITYDIFRNPELEKKGYYVDSLDDLYKQA
DVISLHVPDVPANVHMINDESIAKMKQDVVIVNVSRGPLVDTDAVIRGLD
SGKIFGYAMDVYEGEVGIFNEDWEGKEFPDARLADLIARPNVLVTPHTAF
YTTHAVRNMVVKAFDNNLELVEGKEAETPVKV
3D structure
PDB1j49 Domain closure, substrate specificity and catalysis of D-lactate dehydrogenase from Lactobacillus bulgaricus.
ChainA
Resolution2.2 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 NAD A Y102 I107 G153 G155 I157 Y175 D176 I177 V207 P208 N213 V234 S235 R236 H297 A299 F300 Y102 I107 G153 G155 I157 Y175 D176 I177 V207 P208 N213 V234 S235 R236 H297 A299 F300
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:1j49, PDBe:1j49, PDBj:1j49
PDBsum1j49
PubMed12054772
UniProtP26297|LDHD_LACDA D-lactate dehydrogenase (Gene Name=ldhA)

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