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3D5T

Crystal structure of malate dehydrogenase from Burkholderia pseudomallei

Functional Information from GO Data
ChainGOidnamespacecontents
A0003824molecular_functioncatalytic activity
A0006099biological_processtricarboxylic acid cycle
A0006108biological_processmalate metabolic process
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
B0003824molecular_functioncatalytic activity
B0006099biological_processtricarboxylic acid cycle
B0006108biological_processmalate metabolic process
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
C0003824molecular_functioncatalytic activity
C0006099biological_processtricarboxylic acid cycle
C0006108biological_processmalate metabolic process
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
D0003824molecular_functioncatalytic activity
D0006099biological_processtricarboxylic acid cycle
D0006108biological_processmalate metabolic process
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
Functional Information from PDB Data
site_idAC2
Number of Residues1
DetailsBINDING SITE FOR RESIDUE MG B 401
ChainResidue
BTRP262

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsActive site: {"description":"Proton acceptor","evidences":[{"source":"HAMAP-Rule","id":"MF_01517","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues56
DetailsBinding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_01517","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 1emd
ChainResidueDetails
AASN187
AASP160

site_idCSA2
Number of Residues2
DetailsAnnotated By Reference To The Literature 1emd
ChainResidueDetails
BASN187
BASP160

site_idCSA3
Number of Residues2
DetailsAnnotated By Reference To The Literature 1emd
ChainResidueDetails
CASN187
CASP160

site_idCSA4
Number of Residues2
DetailsAnnotated By Reference To The Literature 1emd
ChainResidueDetails
DASN187
DASP160

site_idCSA5
Number of Residues3
DetailsAnnotated By Reference To The Literature 1emd
ChainResidueDetails
AASP160
AHIS188
AARG163

site_idCSA6
Number of Residues3
DetailsAnnotated By Reference To The Literature 1emd
ChainResidueDetails
BASP160
BHIS188
BARG163

site_idCSA7
Number of Residues3
DetailsAnnotated By Reference To The Literature 1emd
ChainResidueDetails
CASP160
CHIS188
CARG163

site_idCSA8
Number of Residues3
DetailsAnnotated By Reference To The Literature 1emd
ChainResidueDetails
DASP160
DHIS188
DARG163

242842

PDB entries from 2025-10-08

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