Structure of PDB 1hyg Chain B

Receptor sequence

>1hygB (length=313) Species: 2190 (Methanocaldococcus jannaschii)

MKVTIIGASGRVGSATALLLAKEPFMKDLVLIGREHSINKLEGLREDIYD
ALAGTRSDANIYVESDENLRIIDESDVVIITSGVPRKEGMSRMDLAKTNA
KIVGKYAKKIAEICDTKIFVITNPVDVMTYKALVDSKFERNQVFGLGTHL
DSLRFKVAIAKFFGVHIDEVRTRIIGEHGDSMVPLLSATSIGGIPIQKFE
RFKELPIDEIIEDVKTKGEQIIRLKGGSEFGPAAAILNVVRCIVNNEKRL
LTLSAYVDGEFDGIRDVCIGVPVKIGRDGIEEVVSIELDKDEIIAFRKSA
EIIKKYCEEVKNL

3D structure

• PDB: 1hyg Crystal structure of the MJ0490 gene product of the hyperthermophilic archaebacterium Methanococcus jannaschii, a novel member of the lactate/malate family of dehydrogenases
• Chain: B
• Resolution: 2.8 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): R92 D151 R154 H178
• Catalytic site (residue number reindexed from 1): R92 D151 R154 H178
• Enzyme Commision number: 1.1.1.375: L-2-hydroxycarboxylate 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	NAP	B	G7 S9 G10 R11 V12 R34 H36 S37 T81 S82 G83 I102 T122 N123 H178 S228	G7 S9 G10 R11 V12 R34 H36 S37 T81 S82 G83 I102 T122 N123 H178 S228

Gene Ontology

Molecular Function

• GO:0003824 catalytic activity
• GO:0004459 L-lactate dehydrogenase activity
• GO:0016491 oxidoreductase activity
• GO:0016616 oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
• GO:0102443 L-2-hydroxycarboxylate dehydrogenase (NAD+) activity

Biological Process

• GO:0006089 lactate metabolic process
• GO:0006090 pyruvate metabolic process
• GO:0006099 tricarboxylic acid cycle
• GO:0019752 carboxylic acid metabolic process

Cellular Component

• GO:0005737 cytoplasm

External links

• PDB: RCSB:1hyg, PDBe:1hyg, PDBj:1hyg
• PDBsum: 1hyg
• PubMed: 11292347
• UniProt: Q60176|MDH_METJA L-2-hydroxycarboxylate dehydrogenase (NAD(P)(+)) (Gene Name=mdh)