Structure of PDB 1uxh Chain A

Receptor sequence
>1uxhA (length=308) Species: 1108 (Chloroflexus aurantiacus) [Search protein sequence]
RKKISIIGAGFVGSTTAHWLAAKELGDIVLLDIVEGVPQGKALDLYEASP
IEGFDVRVTGTNNYADTANSDVIVVTSGAPRKPGMSREDLIKVNADITRA
CISQAAPLSPNAVIIMVNNPLDAMTYLAAEVSGFPKERVIGQAGVLDAAR
YRTFIAMEAGVSVQDVQAMLMGGHGDEMVPLPRFSTISGIPVSEFIAPDR
LAQIVERTRKGGGEIVNLLKTGSAYYAPAAATAQMVEAVLKDKKRVMPVA
AYLTGQYGLNDIYFGVPVILGAGGVEKILELPLNEEEMALLNASAKAVRA
TLDTLKSL
3D structure
PDB1uxh Large Improvement in the Thermal Stability of a Tetrameric Malate Dehydrogenase by Single Point Mutations at the Dimer-Dimer Interface.
ChainA
Resolution2.1 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) R88 D148 R151 H175
Catalytic site (residue number reindexed from 1) R87 D147 R150 H174
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 G9 G11 F12 V13 D33 T77 S78 G79 A80 P81 C102 V118 N120 Q143 L147 H175 P229 G8 G10 F11 V12 D32 T76 S77 G78 A79 P80 C101 V117 N119 Q142 L146 H174 P228
BS02 FUM A R82 R88 L147 R151 H175 G213 S224 R81 R87 L146 R150 H174 G212 S223
Gene Ontology
Molecular Function
GO:0003824 catalytic 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: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:1uxh, PDBe:1uxh, PDBj:1uxh
PDBsum1uxh
PubMed15321717
UniProtP80040|MDH_CHLAA Malate dehydrogenase (Gene Name=mdh)

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