Structure of PDB 2hlp Chain A

Receptor sequence

>2hlpA (length=303) Species: 2238 (Haloarcula marismortui)

TKVSVVGAAGTVGAAAGYNIALRDIADEVVFVDIPDKEDDTVGQAADTNH
GIAYDSNTRVRQGGYEDTAGSDVVVITAGIPRQPGQTRIDLAGDNAPIME
DIQSSLDEHNDDYISLTTSNPVDLLNRHLYEAGDRSREQVIGFGGRLDSA
RFRYVLSEEFDAPVQNVEGTILGEHGDAQVPVFSKVRVDGTDPEFSGDEK
EQLLGDLQESAMDVIERKGATEWGPARGVAHMVEAILHDTGRVLPASVKL
EGEFGHEDTAFGVPVRLGSNGVEEIVEWDLDDYEQDLMADAAEKLSDQYD
KIS

3D structure

• PDB: 2hlp Halophilic adaptation: novel solvent protein interactions observed in the 2.9 and 2.6 A resolution structures of the wild type and a mutant of malate dehydrogenase from Haloarcula marismortui.
• Chain: A
• Resolution: 2.59 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): R109 D168 R171 H195
• Catalytic site (residue number reindexed from 1): R88 D148 R151 H175
• Enzyme Commision number: 1.1.1.37: malate 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	CL	A	K205 D306	K185 D279

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:0030060 L-malate 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:2hlp, PDBe:2hlp, PDBj:2hlp
• PDBsum: 2hlp
• PubMed: 10653643
• UniProt: Q07841|MDH_HALMA Malate dehydrogenase (Gene Name=mdh)