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2CMD

THE CRYSTAL STRUCTURE OF E.COLI MALATE DEHYDROGENASE: A COMPLEX OF THE APOENZYME AND CITRATE AT 1.87 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
AHOH335
AHOH353
AHOH354
AHOH369
AHOH404
AILE12
AARG81
AARG87
AASN119

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
DetailsAnnotated By Reference To The Literature 1emd
ChainResidueDetails
AHIS177
AASP150

site_idCSA2
Number of Residues3
DetailsAnnotated By Reference To The Literature 1emd
ChainResidueDetails
AHIS177
AASP150
AARG153

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

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PDB entries from 2024-10-30

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