Structure of PDB 2x0r Chain B

Receptor sequence
>2x0rB (length=303) Species: 2238 (Haloarcula marismortui) [Search protein sequence]
TKVSVVGAAGTVGAAAGYNIALRDIADEVVFVDIPDKEDDTVGQAADTNH
GIAYDSNTRVRQGGYEDTAGSDVVVITAGIPRQPGQTRIDLAGDNAPIME
DIQSSLDEHNDDYISLTTSNPVDLLNRHLYEAGDRSREQVIGFGGRLDSA
RFRYVLSEEFDAPVQNVEGTILGEHGDAQVPVFSKVSVDGTDPEFSGDEK
EQLLGDLQESAMDVIERKGATEWGPARGVAHMVEAILHDTGEVLPASVKL
EGEFGHEDTAFGVPVSLGSNGVEEIVEWDLDDYEQDLMADAAEKLSDQYD
KIS
3D structure
PDB2x0r The Oligomeric States of Haloarcula Marismortui Malate Dehydrogenase are Modulated by Solvent Components as Shown by Crystallographic and Biochemical Studies
ChainB
Resolution2.915 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) 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 NAD B G28 G30 T31 V32 D53 T97 A98 G99 R102 T138 S139 N140 F163 H195 G7 G10 T11 V12 D33 T77 A78 G79 R82 T118 S119 N120 F143 H175
BS02 CL B K205 D306 K185 D279
BS03 CL B R43 R252 A255 H256 E259 R23 R227 A230 H231 E234
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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Molecular Function

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Biological Process

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Cellular Component
External links
PDB RCSB:2x0r, PDBe:2x0r, PDBj:2x0r
PDBsum2x0r
PubMed12581646
UniProtQ07841|MDH_HALMA Malate dehydrogenase (Gene Name=mdh)

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