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1HYE

CRYSTAL STRUCTURE OF THE MJ0490 GENE PRODUCT, THE FAMILY OF LACTATE/MALATE DEHYDROGENASE, DIMERIC STRUCTURE

Functional Information from GO Data
ChainGOidnamespacecontents
A0003824molecular_functioncatalytic activity
A0004459molecular_functionL-lactate dehydrogenase (NAD+) activity
A0005737cellular_componentcytoplasm
A0006089biological_processlactate metabolic process
A0006099biological_processtricarboxylic acid cycle
A0016491molecular_functionoxidoreductase activity
A0016616molecular_functionoxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
A0019752biological_processcarboxylic acid metabolic process
A0042867biological_processpyruvate catabolic process
A0102443molecular_functionL-2-hydroxycarboxylate dehydrogenase (NAD+) activity
Functional Information from PDB Data
site_idAC1
Number of Residues25
DetailsBINDING SITE FOR RESIDUE NAP A 748
ChainResidue
AGLY7
ATHR81
AGLY83
AVAL84
AARG86
AILE102
ATYR106
AILE121
ATHR122
AASN123
ALEU146
ASER9
AHIS178
AGLU219
AHOH1003
AHOH1007
AHOH1019
AHOH1046
AGLY10
AARG11
AVAL12
AARG34
AHIS36
ASER37
AASN68

Functional Information from PROSITE/UniProt
site_idPS00064
Number of Residues7
DetailsL_LDH L-lactate dehydrogenase active site. IGEHGDS
ChainResidueDetails
AILE175-SER181

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Proton acceptor => ECO:0000250|UniProtKB:P61889
ChainResidueDetails
AHIS178

site_idSWS_FT_FI2
Number of Residues4
DetailsBINDING: BINDING => ECO:0000269|PubMed:11292347
ChainResidueDetails
AGLY7
AARG34
AASN99
AILE121

site_idSWS_FT_FI3
Number of Residues4
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:P61889
ChainResidueDetails
AARG86
AARG92
AASN123
AARG154

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 1emd
ChainResidueDetails
AASP151
AHIS178

site_idCSA2
Number of Residues3
DetailsAnnotated By Reference To The Literature 1emd
ChainResidueDetails
AASP151
AARG154
AHIS178

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PDB entries from 2025-06-18

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