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1HYG

Crystal structure of MJ0490 gene product, the family of lactate/malate dehydrogenase

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
A0030060molecular_functionL-malate dehydrogenase (NAD+) activity
A0042867biological_processpyruvate catabolic process
A0046554molecular_functionL-malate dehydrogenase (NADP+) activity
A0102443molecular_functionL-2-hydroxycarboxylate dehydrogenase (NAD+) activity
B0003824molecular_functioncatalytic activity
B0004459molecular_functionL-lactate dehydrogenase (NAD+) activity
B0005737cellular_componentcytoplasm
B0006089biological_processlactate metabolic process
B0006099biological_processtricarboxylic acid cycle
B0016491molecular_functionoxidoreductase activity
B0016616molecular_functionoxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
B0019752biological_processcarboxylic acid metabolic process
B0030060molecular_functionL-malate dehydrogenase (NAD+) activity
B0042867biological_processpyruvate catabolic process
B0046554molecular_functionL-malate dehydrogenase (NADP+) activity
B0102443molecular_functionL-2-hydroxycarboxylate dehydrogenase (NAD+) activity
Functional Information from PDB Data
site_idAC1
Number of Residues18
DetailsBINDING SITE FOR RESIDUE NAP A 900
ChainResidue
AGLY7
ATHR81
AGLY83
APRO85
AILE102
ATHR122
AASN123
AHIS178
AGLY227
ASER228
ASER9
AGLY10
AARG11
AVAL12
AGLY33
AARG34
AHIS36
ASER37

site_idAC2
Number of Residues24
DetailsBINDING SITE FOR RESIDUE NAP B 901
ChainResidue
AASP115
BGLY7
BSER9
BGLY10
BARG11
BVAL12
BARG34
BHIS36
BSER37
BTHR81
BSER82
BGLY83
BILE102
BLYS105
BILE121
BTHR122
BASN123
BLEU146
BARG154
BHIS178
BGLY227
BSER228
BHOH736
BHOH758

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 Residues2
DetailsActive site: {"description":"Proton acceptor","evidences":[{"source":"UniProtKB","id":"P61889","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues10
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"11292347","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1HYG","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues2
DetailsBinding site: {"evidences":[{"source":"PDB","id":"1HYG","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues8
DetailsBinding site: {"evidences":[{"source":"UniProtKB","id":"P61889","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues2
DetailsSite: {"description":"Discrimination site allowing the use of NADPH","evidences":[{"source":"PubMed","id":"10998181","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues2
DetailsSite: {"description":"Discrimination site conferring specificity for malate over lactate","evidences":[{"source":"PubMed","id":"10998181","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

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

site_idCSA2
Number of Residues2
DetailsAnnotated By Reference To The Literature 1emd
ChainResidueDetails
BASP151
BHIS178

site_idCSA3
Number of Residues3
DetailsAnnotated By Reference To The Literature 1emd
ChainResidueDetails
AASP151
AARG154
AHIS178

site_idCSA4
Number of Residues3
DetailsAnnotated By Reference To The Literature 1emd
ChainResidueDetails
BASP151
BARG154
BHIS178

249697

PDB entries from 2026-02-25

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