Structure of PDB 1a5z Chain A

Receptor sequence
>1a5zA (length=312) Species: 2336 (Thermotoga maritima) [Search protein sequence]
MKIGIVGLGRVGSSTAFALLMKGFAREMVLIDVDKKRAEGDALDLIHGTP
FTRRANIYAGDYADLKGSDVVIVAAGVPQKPGETRLQLLGRNARVMKEIA
RNVSKYAPDSIVIVVTNPVDVLTYFFLKESGMDPRKVFGSGTVLDTARLR
TLIAQHCGFSPRSVHVYVIGEHGDSEVPVWSGAMIGGIPLQNMCQVCQKC
DSKILENFAEKTKRAAYEIIERKGATHYAIALAVADIVESIFFDEKRVLT
LSVYLEDYLGVKDLCISVPVTLGKHGVERILELNLNEEELEAFRKSASIL
KNAINEITAEEN
3D structure
PDB1a5z Lactate dehydrogenase from the hyperthermophilic bacterium thermotoga maritima: the crystal structure at 2.1 A resolution reveals strategies for intrinsic protein stabilization.
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) R109 D168 R171 H195
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 FBP A R173 S186 H188 G209A R150 S163 H165 G186
BS02 FBP A E60 Y79 D84 D87 E39 Y58 D61 D64
BS03 NAD A G28 G30 R31 V32 D53 V54 A98 G99 T139 N140 A245 T246 G7 G9 R10 V11 D32 V33 A75 G76 T116 N117 A225 T226
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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Cellular Component
External links
PDB RCSB:1a5z, PDBe:1a5z, PDBj:1a5z
PDBsum1a5z
PubMed9655830
UniProtP16115|LDH_THEMA L-lactate dehydrogenase (Gene Name=ldh)

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