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7CGD

Silver-bound E.coli malate dehydrogenase

Functional Information from GO Data
ChainGOidnamespacecontents
A0003824molecular_functioncatalytic activity
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0006096biological_processglycolytic process
A0006099biological_processtricarboxylic acid cycle
A0006108biological_processmalate metabolic process
A0006113biological_processfermentation
A0009061biological_processanaerobic 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
A0019898cellular_componentextrinsic component of membrane
A0030060molecular_functionL-malate dehydrogenase (NAD+) activity
A0042803molecular_functionprotein homodimerization activity
B0003824molecular_functioncatalytic activity
B0005737cellular_componentcytoplasm
B0005829cellular_componentcytosol
B0006096biological_processglycolytic process
B0006099biological_processtricarboxylic acid cycle
B0006108biological_processmalate metabolic process
B0006113biological_processfermentation
B0009061biological_processanaerobic 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
B0019898cellular_componentextrinsic component of membrane
B0030060molecular_functionL-malate dehydrogenase (NAD+) activity
B0042803molecular_functionprotein homodimerization activity
C0003824molecular_functioncatalytic activity
C0005737cellular_componentcytoplasm
C0005829cellular_componentcytosol
C0006096biological_processglycolytic process
C0006099biological_processtricarboxylic acid cycle
C0006108biological_processmalate metabolic process
C0006113biological_processfermentation
C0009061biological_processanaerobic 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
C0019898cellular_componentextrinsic component of membrane
C0030060molecular_functionL-malate dehydrogenase (NAD+) activity
C0042803molecular_functionprotein homodimerization activity
D0003824molecular_functioncatalytic activity
D0005737cellular_componentcytoplasm
D0005829cellular_componentcytosol
D0006096biological_processglycolytic process
D0006099biological_processtricarboxylic acid cycle
D0006108biological_processmalate metabolic process
D0006113biological_processfermentation
D0009061biological_processanaerobic 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
D0019898cellular_componentextrinsic component of membrane
D0030060molecular_functionL-malate dehydrogenase (NAD+) activity
D0042803molecular_functionprotein homodimerization activity
Functional Information from PDB Data
site_idAC1
Number of Residues5
Detailsbinding site for residue AG A 401
ChainResidue
AGLY69
AALA70
ACYS109
AAG402
AHOH512

site_idAC2
Number of Residues4
Detailsbinding site for residue AG A 402
ChainResidue
ATHR108
ACYS109
AAG401
AHOH511

site_idAC3
Number of Residues5
Detailsbinding site for residue AG A 403
ChainResidue
AASP71
ALYS111
ACYS113
ALEU242
AAG404

site_idAC4
Number of Residues5
Detailsbinding site for residue AG A 404
ChainResidue
ALYS111
ACYS113
ALYS142
AASN273
AAG403

site_idAC5
Number of Residues4
Detailsbinding site for residue AG A 405
ChainResidue
APRO172
AVAL173
ACYS251
AAG406

site_idAC6
Number of Residues3
Detailsbinding site for residue AG A 406
ChainResidue
ACYS251
AAG405
AHOH513

site_idAC7
Number of Residues4
Detailsbinding site for residue AG A 407
ChainResidue
AASN119
AHIS177
AMET227
AHOH509

site_idAC8
Number of Residues5
Detailsbinding site for residue AG B 401
ChainResidue
BGLY69
BALA70
BCYS109
BAG402
BHOH513

site_idAC9
Number of Residues4
Detailsbinding site for residue AG B 402
ChainResidue
BTHR108
BCYS109
BAG401
BHOH513

site_idAD1
Number of Residues6
Detailsbinding site for residue AG B 403
ChainResidue
BASP71
BCYS113
BLEU242
BAG404
BAG405
BHOH512

site_idAD2
Number of Residues5
Detailsbinding site for residue AG B 404
ChainResidue
BLYS111
BCYS113
BLYS142
BASN273
BAG403

site_idAD3
Number of Residues5
Detailsbinding site for residue AG B 405
ChainResidue
BCYS113
BLEU238
BLEU242
BGLY274
BAG403

site_idAD4
Number of Residues3
Detailsbinding site for residue AG B 406
ChainResidue
BCYS251
BAG407
BHOH511

site_idAD5
Number of Residues4
Detailsbinding site for residue AG B 407
ChainResidue
BPRO172
BVAL173
BCYS251
BAG406

site_idAD6
Number of Residues3
Detailsbinding site for residue AG B 408
ChainResidue
BASN119
BHIS177
BMET227

site_idAD7
Number of Residues5
Detailsbinding site for residue AG C 401
ChainResidue
CLYS111
CCYS113
CLYS142
CASN273
CAG402

site_idAD8
Number of Residues5
Detailsbinding site for residue AG C 402
ChainResidue
CASP71
CCYS113
CLEU242
CAG401
CHOH509

site_idAD9
Number of Residues4
Detailsbinding site for residue AG C 403
ChainResidue
CCYS113
CLEU238
CLEU242
CGLY274

site_idAE1
Number of Residues4
Detailsbinding site for residue AG C 404
ChainResidue
CPRO172
CVAL173
CCYS251
CAG405

site_idAE2
Number of Residues3
Detailsbinding site for residue AG C 405
ChainResidue
CCYS251
CAG404
CHOH510

site_idAE3
Number of Residues4
Detailsbinding site for residue AG C 406
ChainResidue
CASN119
CHIS177
CMET227
CHOH508

site_idAE4
Number of Residues6
Detailsbinding site for residue AG D 401
ChainResidue
DGLY69
DALA70
DCYS109
DAG402
DHOH510
DHOH513

site_idAE5
Number of Residues4
Detailsbinding site for residue AG D 402
ChainResidue
DHOH513
DTHR108
DCYS109
DAG401

site_idAE6
Number of Residues4
Detailsbinding site for residue AG D 403
ChainResidue
DASP71
DCYS113
DAG404
DHOH508

site_idAE7
Number of Residues6
Detailsbinding site for residue AG D 404
ChainResidue
DCYS113
DLEU238
DLEU242
DGLY274
DAG403
DHOH501

site_idAE8
Number of Residues3
Detailsbinding site for residue AG D 405
ChainResidue
DCYS251
DAG406
DHOH512

site_idAE9
Number of Residues4
Detailsbinding site for residue AG D 406
ChainResidue
DPRO172
DVAL173
DCYS251
DAG405

Functional Information from PROSITE/UniProt
site_idPS00068
Number of Residues13
DetailsMDH Malate dehydrogenase active site signature. VTTLDiiRSntfV
ChainResidueDetails
AVAL146-VAL158

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsActive site: {"description":"Proton acceptor","evidences":[{"source":"HAMAP-Rule","id":"MF_01516","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"11389141","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues44
DetailsBinding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_01516","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"11389141","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8331658","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues8
DetailsBinding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_01516","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"1507230","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"8331658","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idMCSA1
Number of Residues2
DetailsM-CSA 527
ChainResidueDetails
AASP150modifies pKa
AHIS177proton acceptor, proton donor

site_idMCSA2
Number of Residues2
DetailsM-CSA 527
ChainResidueDetails
BASP150modifies pKa
BHIS177proton acceptor, proton donor

site_idMCSA3
Number of Residues2
DetailsM-CSA 527
ChainResidueDetails
CASP150modifies pKa
CHIS177proton acceptor, proton donor

site_idMCSA4
Number of Residues2
DetailsM-CSA 527
ChainResidueDetails
DASP150modifies pKa
DHIS177proton acceptor, proton donor

238895

PDB entries from 2025-07-16

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