Structure of PDB 2xxj Chain D

Receptor sequence
>2xxjD (length=310) Species: 300852 (Thermus thermophilus HB8) [Search protein sequence]
MKVGIVGSGMVGSATAYALALLGVAREVVLVDLDRKLAQAHAEDILHATP
FAHPVWVWAGSYGDLEGARAVVLAAGVAQRPGETRLQLLDRNAQVFAQVV
PRVLEAAPEAVLLVATNPVDVMTQVAYALSGLPPGRVVGSGTILDTARFR
ALLAEYLRVAPQSVHAYVLGEHGDSEVLVWSSAQVGGVPLLEFAEARGRA
LSPEDRARIDEGVRRAAYRIIEGKGATYYGIGAGLARLVRAILTDEKGVY
TVSAFTPEVAGVLEVSLSLPRILGAGGVAGTVYPSLSPEERAALRRSAEI
LKEAAFALGF
3D structure
PDB2xxj Lactate Dehydrogenase from T. Thermophilus, Penta- Mutant (Ternary Complex)
ChainD
Resolution1.964 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) R85 D145 R148 H172
Catalytic site (residue number reindexed from 1) R85 D145 R148 H172
Enzyme Commision number 1.1.1.27: L-lactate 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 D G7 G9 M10 V11 D32 L33 Y62 A75 G76 V77 A78 V99 A115 N117 H172 T227 I231 G7 G9 M10 V11 D32 L33 Y62 A75 G76 V77 A78 V99 A115 N117 H172 T227 I231
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
Biological Process
GO:0006089 lactate metabolic process
GO:0006090 pyruvate metabolic process
GO:0006096 glycolytic process
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:2xxj, PDBe:2xxj, PDBj:2xxj
PDBsum2xxj
PubMed
UniProtQ5SJA1|LDH_THET8 L-lactate dehydrogenase (Gene Name=ldh)

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