Structure of PDB 6sbv Chain F

Receptor sequence
>6sbvF (length=329) Species: 9606 (Homo sapiens) [Search protein sequence]
ATLKDQLIYNLLKQTPQNKITVVGVGAVGMACAISILMKDLADELALVDV
IEDKLKGEMMDLQHGSLFLRTPKIVSGKDYNVTANSKLVIITAGARQQEG
ESRLNLVQRNVNIFKFIIPNVVKYSPNCKLLIVSNPVDILTYVAWKISGF
PKNRVIGSGCNLDSARFRYLMGERLGVHPLSCHGWVLGEHGDSSVPVWSG
MNVAGVSLKTLHPDLGTDKDKEQWKEVHKQVVESAYEVIKLKGYTSWAIG
LSVADLAESIMKNLRRVHPVSTMIKGLYGIKDDVFLSVPCILGQNGISDL
VKVTLTSEEEARLKKSADTLWGIQKELQF
3D structure
PDB6sbv Structural Evidence for Isoform-Selective Allosteric Inhibition of Lactate Dehydrogenase A.
ChainF
Resolution2.6 Å
3D
structure
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Enzymatic activity
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 L5K F Q66 H67 L70 T74 P75 I77 Q63 H64 L67 T71 P72 I74
BS02 L5K F R169 Y172 L173 G179 V180 S237 R166 Y169 L170 G176 V177 S234
Gene Ontology
Molecular Function
GO:0003824 catalytic activity
GO:0004459 L-lactate dehydrogenase activity
GO:0005515 protein binding
GO:0016491 oxidoreductase activity
GO:0016616 oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
GO:0042802 identical protein binding
GO:0045296 cadherin 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:0005634 nucleus
GO:0005737 cytoplasm
GO:0005739 mitochondrion
GO:0005829 cytosol
GO:0016020 membrane
GO:0070062 extracellular exosome
GO:1990204 oxidoreductase complex

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Molecular Function
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Cellular Component
External links
PDB RCSB:6sbv, PDBe:6sbv, PDBj:6sbv
PDBsum6sbv
PubMed32548488
UniProtP00338|LDHA_HUMAN L-lactate dehydrogenase A chain (Gene Name=LDHA)

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