Structure of PDB 4ln1 Chain B

Receptor sequence
>4ln1B (length=321) Species: 226900 (Bacillus cereus ATCC 14579) [Search protein sequence]
ENLYFQSMKKGINRVVLVGTGAVGCSYAYCMINQAVAEEFVLVDVNEAKA
EGEAMDLSHAVPFAPAPTRVWKGSYEDCKDADLVVITAGLPQKPGETRLD
LVEKNAKIFKQIVRSIMDSGFDGIFLIATNPVDILTYVTWKESGLPKERV
IGSGTTLDSARFRYMLGEYFDIGPHNIHAYIIGEHGDTELPVWSHVSVGI
QKLQTLLEKDNTYNQEDLDKIFINVRDAAYHIIERKGATYYGIGMSLLRV
TKAILNDENSVLTVSAYLEGQYGQKDVYIGVPAVLNRGGVREILEVELSE
DEELKFDHSVQVLKETMAPVL
3D structure
PDB4ln1 Crystal structure of L-lactate dehydrogenase from Bacillus cereus ATCC 14579 complexed with calcium, NYSGRC Target 029452
ChainB
Resolution1.9 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) R91 D151 R154 H178
Catalytic site (residue number reindexed from 1) R98 D158 R161 H185
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 CA B K3 I5 D75 K10 I12 D82
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:4ln1, PDBe:4ln1, PDBj:4ln1
PDBsum4ln1
PubMed
UniProtQ81EP4|LDH1_BACCR L-lactate dehydrogenase 1 (Gene Name=ldh1)

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