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SummaryStructural detailsExperimental detailsFunctional detailsSequence NeighborHistoryDownloads

4WLE

Crystal structure of citrate bound MDH2

Functional Information from GO Data
ChainGOidnamespacecontents
A0003723molecular_functionRNA binding
A0003824molecular_functioncatalytic activity
A0005634cellular_componentnucleus
A0005737cellular_componentcytoplasm
A0005739cellular_componentmitochondrion
A0005759cellular_componentmitochondrial matrix
A0006094biological_processgluconeogenesis
A0006099biological_processtricarboxylic acid cycle
A0006108biological_processmalate metabolic process
A0009060biological_processaerobic respiration
A0016020cellular_componentmembrane
A0016491molecular_functionoxidoreductase activity
A0016615molecular_functionmalate dehydrogenase 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
A0042802molecular_functionidentical protein binding
A0043490biological_processmalate-aspartate shuttle
A0046554molecular_functionL-malate dehydrogenase (NADP+) activity
A0070062cellular_componentextracellular exosome
B0003723molecular_functionRNA binding
B0003824molecular_functioncatalytic activity
B0005634cellular_componentnucleus
B0005737cellular_componentcytoplasm
B0005739cellular_componentmitochondrion
B0005759cellular_componentmitochondrial matrix
B0006094biological_processgluconeogenesis
B0006099biological_processtricarboxylic acid cycle
B0006108biological_processmalate metabolic process
B0009060biological_processaerobic respiration
B0016020cellular_componentmembrane
B0016491molecular_functionoxidoreductase activity
B0016615molecular_functionmalate dehydrogenase 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
B0042802molecular_functionidentical protein binding
B0043490biological_processmalate-aspartate shuttle
B0046554molecular_functionL-malate dehydrogenase (NADP+) activity
B0070062cellular_componentextracellular exosome
C0003723molecular_functionRNA binding
C0003824molecular_functioncatalytic activity
C0005634cellular_componentnucleus
C0005737cellular_componentcytoplasm
C0005739cellular_componentmitochondrion
C0005759cellular_componentmitochondrial matrix
C0006094biological_processgluconeogenesis
C0006099biological_processtricarboxylic acid cycle
C0006108biological_processmalate metabolic process
C0009060biological_processaerobic respiration
C0016020cellular_componentmembrane
C0016491molecular_functionoxidoreductase activity
C0016615molecular_functionmalate dehydrogenase activity
C0016616molecular_functionoxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
C0019752biological_processcarboxylic acid metabolic process
C0030060molecular_functionL-malate dehydrogenase (NAD+) activity
C0042802molecular_functionidentical protein binding
C0043490biological_processmalate-aspartate shuttle
C0046554molecular_functionL-malate dehydrogenase (NADP+) activity
C0070062cellular_componentextracellular exosome
D0003723molecular_functionRNA binding
D0003824molecular_functioncatalytic activity
D0005634cellular_componentnucleus
D0005737cellular_componentcytoplasm
D0005739cellular_componentmitochondrion
D0005759cellular_componentmitochondrial matrix
D0006094biological_processgluconeogenesis
D0006099biological_processtricarboxylic acid cycle
D0006108biological_processmalate metabolic process
D0009060biological_processaerobic respiration
D0016020cellular_componentmembrane
D0016491molecular_functionoxidoreductase activity
D0016615molecular_functionmalate dehydrogenase activity
D0016616molecular_functionoxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
D0019752biological_processcarboxylic acid metabolic process
D0030060molecular_functionL-malate dehydrogenase (NAD+) activity
D0042802molecular_functionidentical protein binding
D0043490biological_processmalate-aspartate shuttle
D0046554molecular_functionL-malate dehydrogenase (NADP+) activity
D0070062cellular_componentextracellular exosome
Functional Information from PDB Data
site_idAC1
Number of Residues11
Detailsbinding site for residue CIT A 401
ChainResidue
AARG104
AHOH512
AHOH536
AARG110
AILE140
AASN142
AARG176
AHIS200
AGLY234
AALA247
AMET251
site_idAC2
Number of Residues9
Detailsbinding site for residue CIT B 401
ChainResidue
BARG104
BARG110
BASN142
BARG176
BHIS200
BGLY234
BALA247
BMET251
BHOH512
site_idAC3
Number of Residues9
Detailsbinding site for residue CIT C 401
ChainResidue
CARG104
CARG110
CILE140
CASN142
CARG176
CHIS200
CGLY234
CALA247
CMET251
site_idAC4
Number of Residues10
Detailsbinding site for residue CIT D 401
ChainResidue
DARG104
DARG110
DILE140
DASN142
DARG176
DHIS200
DGLY234
DALA247
DHOH504
DHOH507
Functional Information from PROSITE/UniProt
site_idPS00068
Number of Residues13
DetailsMDH Malate dehydrogenase active site signature. VTTLDivRAntfV
ChainResidueDetails
AVAL169-VAL181
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsActive site: {"description":"Proton acceptor","evidences":[{"source":"UniProtKB","id":"P00346","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI2
Number of Residues44
DetailsBinding site: {"evidences":[{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"MAR-2006","submissionDatabase":"PDB data bank","title":"Crystal structure of human malate dehydrogenase type 2.","authoringGroup":["Structural genomics consortium (SGC)"]}}]}
ChainResidueDetails
site_idSWS_FT_FI3
Number of Residues16
DetailsBinding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU10004","evidenceCode":"ECO:0000255"},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"MAR-2006","submissionDatabase":"PDB data bank","title":"Crystal structure of human malate dehydrogenase type 2.","authoringGroup":["Structural genomics consortium (SGC)"]}}]}
ChainResidueDetails
site_idSWS_FT_FI4
Number of Residues36
DetailsModified residue: {"description":"N6-succinyllysine; alternate","evidences":[{"source":"UniProtKB","id":"P08249","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI5
Number of Residues4
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"19608861","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI6
Number of Residues8
DetailsModified residue: {"description":"N6-succinyllysine","evidences":[{"source":"UniProtKB","id":"P08249","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI7
Number of Residues12
DetailsModified residue: {"description":"N6-succinyllysine; alternate","evidences":[{"source":"UniProtKB","id":"Q32LG3","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI8
Number of Residues8
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI9
Number of Residues4
DetailsModified residue: {"description":"N6-malonyllysine; alternate","evidences":[{"source":"UniProtKB","id":"Q32LG3","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI10
Number of Residues4
DetailsGlycosylation: {"description":"O-linked (GlcNAc) serine","evidences":[{"source":"UniProtKB","id":"P04636","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

246704

PDB entries from 2025-12-24

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