Structure of PDB 1dxy Chain A

Receptor sequence

>1dxyA (length=330) Species: 1582 (Lacticaseibacillus casei)

MKIIAYGARVDEIQYFKQWAKDTGNTLEYHTEFLDENTVEWAKGFDGINS
LQTTPYAAGVFEKMHAYGIKFLTIRNVGTDNIDMTAMKQYGIRLSNVPAY
SPAAIAEFALTDTLYLLRNMGKVQAQLQAGDYEKAGTFIGKELGQQTVGV
MGTGHIGQVAIKLFKGFGAKVIAYDPYPMKGDHPDFDYVSLEDLFKQSDV
IDLHVPGIEQNTHIINEAAFNLMKPGAIVINTARPNLIDTQAMLSNLKSG
KLAGVGIDTYEYETEDLLNLAKHGSFKDPLWDELLGMPNVVLSPHIAYYT
ETAVHNMVYFSLQHLVDFLTKGETSTEVTG

3D structure

• PDB: 1dxy Crystal structure of a ternary complex of D-2-hydroxyisocaproate dehydrogenase from Lactobacillus casei, NAD+ and 2-oxoisocaproate at 1.9 A resolution.
• Chain: A
• Resolution: 1.86 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): S101 R234 D258 E263 H295
• Catalytic site (residue number reindexed from 1): S101 R234 D258 E263 H295
• Enzyme Commision number: 1.1.1.-

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	Y100 G152 G154 H155 I156 Y174 D175 P176 H204 V205 P206 N211 T232 A233 R234 H295 Y298	Y100 G152 G154 H155 I156 Y174 D175 P176 H204 V205 P206 N211 T232 A233 R234 H295 Y298
BS02	COI	A	V77 Y100 Y298	V77 Y100 Y298

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
• GO:0097256 phenyllactate dehydrogenase (NAD+) activity

External links

• PDB: RCSB:1dxy, PDBe:1dxy, PDBj:1dxy
• PDBsum: 1dxy
• PubMed: 9126843
• UniProt: P17584|DHD2_LACPA D-2-hydroxyisocaproate dehydrogenase