Structure of PDB 3zzn Chain D

Receptor sequence
>3zznD (length=310) Species: 300852 (Thermus thermophilus HB8) [Search protein sequence]
MKVGIVGSGMVGSATAYALALLGVAREVVLVDLDRKLAQAHAEDILHATP
FAHPVWVWAGSYGDLEGARAVVLAAGVAQRPGETRLQLLDRNAQVFAQVV
PRVLEAAPEAVLLVATNPVDVMTQVAYALSGLPPGRVVGSGTILDTARFR
ALLAEYLRVAPQSVHAYVLGEHGDSEVLVWSSAQVGGVPLLEFAEARGRA
LSPEDRARIDEGVRRAAYRIIEGKGATYYGIGAGLARLVRAILTDEKGVY
TVSAFTPEVAGVLEVSLSLPRILGAGGVAGTVYPSLSPEERAALRRSAEI
LKEAAFALGF
3D structure
PDB3zzn Sampling the conformational energy landscape of a hyperthermophilic protein by engineering key substitutions.
ChainD
Resolution2.9 Å
3D
structure
Catalytic site residues are labeled in the structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]
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 ADP D G30 V32 D53 L54 A98 G99 V119 G9 V11 D32 L33 A75 G76 V95
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

View graph for
Molecular Function
View graph for
Biological Process
View graph for
Cellular Component
External links
PDB RCSB:3zzn, PDBe:3zzn, PDBj:3zzn
PDBsum3zzn
PubMed22319152
UniProtQ5SJA1|LDH_THET8 L-lactate dehydrogenase (Gene Name=ldh)

[Back to BioLiP]