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1EMD

CRYSTAL STRUCTURE OF A TERNARY COMPLEX OF ESCHERICHIA COLI MALATE DEHYDROGENASE, CITRATE AND NAD AT 1.9 ANGSTROMS RESOLUTION

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
Functional Information from PDB Data
site_idAC1
Number of Residues12
DetailsBINDING SITE FOR RESIDUE CIT A 313
ChainResidue
AARG153
AHIS177
AGLY210
AALA223
ANAD314
AHOH349
AHOH350
AHOH398
AILE12
AARG81
AARG87
AASN119

site_idAC2
Number of Residues27
DetailsBINDING SITE FOR RESIDUE NAD A 314
ChainResidue
AALA9
AGLY10
AGLY11
AILE12
ATYR33
AASP34
AILE35
ASER76
AALA77
AGLY78
AVAL79
AARG80
AASN94
AILE117
ATHR118
AASN119
AVAL121
AVAL146
AHIS177
ATHR224
AMET227
ACIT313
AHOH316
AHOH332
AHOH342
AHOH398
AHOH399

site_idACT
Number of Residues5
Details
ChainResidue
AARG81
AARG87
AASP150
AARG153
AHIS177

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 Residues1
DetailsACT_SITE: Proton acceptor => ECO:0000255|HAMAP-Rule:MF_01516, ECO:0000305|PubMed:11389141
ChainResidueDetails
AHIS177

site_idSWS_FT_FI2
Number of Residues5
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_01516, ECO:0000269|PubMed:11389141, ECO:0000269|PubMed:8331658
ChainResidueDetails
AGLY7
AASP34
AASN94
AILE117
AMET227

site_idSWS_FT_FI3
Number of Residues4
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_01516, ECO:0000305|PubMed:1507230, ECO:0000305|PubMed:8331658
ChainResidueDetails
AARG81
AARG87
AASN119
AARG153

Catalytic Information from CSA
site_idCSA1
Number of Residues2
Detailsa catalytic site defined by CSA, PubMed 8331658, 6848515, 7849603
ChainResidueDetails
AHIS177
AASP150

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

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PDB entries from 2025-06-18

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