Loading
PDBj
MenuPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDBDonate
RCSB PDBPDBeBMRBAdv. SearchSearch help

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
DetailsACT_SITE: Proton acceptor => ECO:0000255|HAMAP-Rule:MF_01517
ChainResidueDetails
AHIS188
BHIS188
CHIS188
DHIS188

site_idSWS_FT_FI2
Number of Residues32
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_01517
ChainResidueDetails
AGLY12
BARG93
BARG99
BASN106
BGLN113
BVAL130
BASN132
BARG163
CGLY12
CARG93
CARG99
AARG93
CASN106
CGLN113
CVAL130
CASN132
CARG163
DGLY12
DARG93
DARG99
DASN106
DGLN113
AARG99
DVAL130
DASN132
DARG163
AASN106
AGLN113
AVAL130
AASN132
AARG163
BGLY12

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

237735

PDB entries from 2025-06-18

PDB statisticsPDBj update infoContact PDBjnumon