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5NQB

Rabbit Muscle L-lactate dehydrogenase in complex with malonate

Functional Information from GO Data
ChainGOidnamespacecontents
A0003824molecular_functioncatalytic activity
A0004459molecular_functionL-lactate dehydrogenase (NAD+) activity
A0005737cellular_componentcytoplasm
A0006089biological_processlactate metabolic process
A0016491molecular_functionoxidoreductase activity
A0016616molecular_functionoxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
A0019752biological_processcarboxylic acid metabolic process
B0003824molecular_functioncatalytic activity
B0004459molecular_functionL-lactate dehydrogenase (NAD+) activity
B0005737cellular_componentcytoplasm
B0006089biological_processlactate metabolic process
B0016491molecular_functionoxidoreductase activity
B0016616molecular_functionoxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
B0019752biological_processcarboxylic acid metabolic process
C0003824molecular_functioncatalytic activity
C0004459molecular_functionL-lactate dehydrogenase (NAD+) activity
C0005737cellular_componentcytoplasm
C0006089biological_processlactate metabolic process
C0016491molecular_functionoxidoreductase activity
C0016616molecular_functionoxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
C0019752biological_processcarboxylic acid metabolic process
D0003824molecular_functioncatalytic activity
D0004459molecular_functionL-lactate dehydrogenase (NAD+) activity
D0005737cellular_componentcytoplasm
D0006089biological_processlactate metabolic process
D0016491molecular_functionoxidoreductase activity
D0016616molecular_functionoxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
D0019752biological_processcarboxylic acid metabolic process
Functional Information from PDB Data
site_idAC1
Number of Residues10
Detailsbinding site for residue MLI A 401
ChainResidue
AARG170
CHOH562
AHIS185
AVAL269
AHOH524
AHOH568
AHOH581
AHOH637
CSER183
CHIS185

site_idAC2
Number of Residues10
Detailsbinding site for residue MLI B 401
ChainResidue
BARG170
BHIS185
BVAL269
BHOH529
BHOH572
BHOH589
BHOH602
BHOH638
DSER183
DHIS185

site_idAC3
Number of Residues6
Detailsbinding site for residue MLI B 402
ChainResidue
BASN137
BLEU164
BARG168
BHIS192
BHOH513
BHOH527

site_idAC4
Number of Residues11
Detailsbinding site for residue MLI C 401
ChainResidue
ASER183
AHIS185
CARG170
CHIS185
CVAL269
CHOH526
CHOH554
CHOH584
CHOH629
CHOH631
CHOH698

site_idAC5
Number of Residues6
Detailsbinding site for residue MLI C 402
ChainResidue
CGLN99
CARG105
CASN137
CARG168
CHIS192
CTHR247

site_idAC6
Number of Residues10
Detailsbinding site for residue MLI D 401
ChainResidue
BSER183
BHIS185
BHOH575
DARG170
DHIS185
DVAL269
DHOH544
DHOH629
DHOH630
DHOH670

site_idAC7
Number of Residues8
Detailsbinding site for residue MLI D 402
ChainResidue
DASN137
DARG168
DHIS192
DALA237
DTHR247
DHOH523
DHOH626
DHOH653

Functional Information from PROSITE/UniProt
site_idPS00064
Number of Residues7
DetailsL_LDH L-lactate dehydrogenase active site. LGEHGDS
ChainResidueDetails
ALEU189-SER195

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsActive site: {"description":"Proton acceptor","evidences":[{"source":"PubMed","id":"19715328","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues132
DetailsBinding site: {}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues4
DetailsModified residue: {"description":"N-acetylalanine","evidences":[{"source":"UniProtKB","id":"P00338","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues12
DetailsModified residue: {"description":"N6-succinyllysine; alternate","evidences":[{"source":"UniProtKB","id":"P06151","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues12
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"P00338","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues4
DetailsModified residue: {"description":"N6-acetyllysine; alternate","evidences":[{"source":"UniProtKB","id":"P00338","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues12
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"P06151","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI8
Number of Residues4
DetailsModified residue: {"description":"Phosphotyrosine","evidences":[{"source":"UniProtKB","id":"P06151","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI9
Number of Residues8
DetailsModified residue: {"description":"Phosphothreonine","evidences":[{"source":"UniProtKB","id":"P04642","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI10
Number of Residues4
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P00338","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI11
Number of Residues8
DetailsCross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate","evidences":[{"source":"UniProtKB","id":"P00338","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

239492

PDB entries from 2025-07-30

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