Structure of PDB 1ldn Chain C

Receptor sequence
>1ldnC (length=316) Species: 1422 (Geobacillus stearothermophilus) [Search protein sequence]
MKNNGGARVVVIGAGFVGASYVFALMNQGIADEIVLIDANESKAIGDAMD
FNHGKVFAPKPVDIWHGDYDDCRDADLVVICAGANQKPGETRLDLVDKNI
AIFRSIVESVMASGFQGLFLVATNPVDILTYATWKFSGLPHERVIGSGTI
LDTARFRFLLGEYFSVAPQNVHAYIIGEHGDTELPVWSQAYIGVMPIRKL
VESKGEEAQKDLERIFVNVRDAAYQIIEKKGATYYGIAMGLARVTRAILH
NENAILTVSAYLDGLYGERDVYIGVPAVINRNGIREVIEIELNDDEKNRF
HHSAATLKSVLARAFT
3D structure
PDB1ldn Structure of a ternary complex of an allosteric lactate dehydrogenase from Bacillus stearothermophilus at 2.5 A resolution.
ChainC
Resolution2.5 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) R92 D152 R155 H179
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 C N184 H186 N170 H172
BS02 NAD C G29 F30 V31 D52 A53 A96 G97 A98 N99 I120 A136 T137 N138 V140 H193 T247 I251 G15 F16 V17 D38 A39 A82 G83 A84 N85 I106 A122 T123 N124 V126 H179 T233 I237
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:0051287 NAD binding
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:1ldn, PDBe:1ldn, PDBj:1ldn
PDBsum1ldn
PubMed1731077
UniProtP00344|LDH_GEOSE L-lactate dehydrogenase (Gene Name=ldh)

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