Structure of PDB 1o6z Chain D

Receptor sequence
>1o6zD (length=298) Species: 2238 (Haloarcula marismortui) [Search protein sequence]
TKVSVVGAAGTVGAAAGYNIALRDIADEVVFVDIPDKEDDTVGQAADTNH
GIAYDSNTRVRQGGYEDTAGSDVVVITAGIQTRIDLAGDNAPIMEDIQSS
LDEHNDDYISLTTSNPVDLLNRHLYEAGDRSREQVIGFGGRLDSARFRYV
LSEEFDAPVQNVEGTILGEHGDAQVPVFSKVSVDGTDPEFSGDEKEQLLG
DLQESAMDVIERKGATEWGPARGVAHMVEAILHDTGEVLPASVKLEGEFG
HEDTAFGVPVSLGSNGVEEIVEWDLDDYEQDLMADAAEKLSDQYDKIS
3D structure
PDB1o6z The Oligomeric States of Haloarcula Marismortui Malate Dehydrogenase are Modulated by Solvent Components as Shown by Crystallographic and Biochemical Studies
ChainD
Resolution1.95 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) R109 D168 R171 H195
Catalytic site (residue number reindexed from 1) R83 D143 R146 H170
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 D K205 D306 K180 D274
BS02 CL D R252 H256 R222 H226
BS03 NAD D A29B G30 T31 V32 D53 I54A K55 T97 A98 T138 N140 H195 A9 G10 T11 V12 D33 I34 K37 T77 A78 T113 N115 H170
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

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Cellular Component
External links
PDB RCSB:1o6z, PDBe:1o6z, PDBj:1o6z
PDBsum1o6z
PubMed12581646
UniProtQ07841|MDH_HALMA Malate dehydrogenase (Gene Name=mdh)

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