Structure of PDB 1hlp Chain A

Receptor sequence
>1hlpA (length=303) Species: 2238 (Haloarcula marismortui) [Search protein sequence]
TKVSVVGAAGTVGAAAGYNIALRDIADEVVFVDIPDKEDDTVGQAADTNH
GIAYDSNTRVRQGGYEDTAGSDVVVITAGIPRQPGQTRIDLAGDNAPIME
DIQSSLDEHNDDYISLTTSNPVDLLNRHLYEAGDRSREQVIGFGGRLDSA
RFRYVLSEEFDAPVQNVEGTILGEHGDAQVPVFSKVRVDGTDPEFSGDEK
EQLLGDLQESAMDVIERKGATEWGPARGVAHMVEAILHDTGEVLPASVKL
EGEFGHEDTAFGVPVRLGSNGVEEIVEWDLDDYEQDLMADAAEKLSDQYD
KIS
3D structure
PDB1hlp Structural Features That Stabilize Halophilic Malate Dehydrogenase from an Archaebacterium.
ChainA
Resolution3.2 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) R106 D166 R169 H193
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 A G27 G29 T30 V31 D52 I53 K54 Y83 T95 A96 I120 T136 N138 V140 F161 G162 H193 T245 P249 G7 G10 T11 V12 D33 I34 K37 Y65 T77 A78 I102 T118 N120 V122 F143 G144 H175 T221 P225
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:1hlp, PDBe:1hlp, PDBj:1hlp
PDBsum1hlp
PubMed17812611
UniProtQ07841|MDH_HALMA Malate dehydrogenase (Gene Name=mdh)

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