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2J5K

2.0 A resolution structure of the wild type malate dehydrogenase from Haloarcula marismortui (radiation damage series)

Functional Information from GO Data
ChainGOidnamespacecontents
A0003824molecular_functioncatalytic activity
A0004459molecular_functionL-lactate dehydrogenase (NAD+) activity
A0005737cellular_componentcytoplasm
A0006089biological_processlactate metabolic process
A0006099biological_processtricarboxylic acid cycle
A0016491molecular_functionoxidoreductase 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
B0004459molecular_functionL-lactate dehydrogenase (NAD+) activity
B0005737cellular_componentcytoplasm
B0006089biological_processlactate metabolic process
B0006099biological_processtricarboxylic acid cycle
B0016491molecular_functionoxidoreductase 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
C0004459molecular_functionL-lactate dehydrogenase (NAD+) activity
C0005737cellular_componentcytoplasm
C0006089biological_processlactate metabolic process
C0006099biological_processtricarboxylic acid cycle
C0016491molecular_functionoxidoreductase 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
D0004459molecular_functionL-lactate dehydrogenase (NAD+) activity
D0005737cellular_componentcytoplasm
D0006089biological_processlactate metabolic process
D0006099biological_processtricarboxylic acid cycle
D0016491molecular_functionoxidoreductase 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_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CL A1331
ChainResidue
ALYS205
AASP306
DTHR210
DASP211

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CL A1332
ChainResidue
ATHR210
AASP211
AHOH2073
DLYS205
DASP306

site_idAC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CL A1333
ChainResidue
AARG166
AARG252
AHIS256
BASP73
BHOH2037

site_idAC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CL B1331
ChainResidue
BLYS205
BASP306
CTHR210
CASP211

site_idAC5
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CL B1332
ChainResidue
ATYR72
AASP73
AHOH2049
BARG166
BARG252
BHIS256

site_idAC6
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CL C1331
ChainResidue
BTHR210
BASP211
CLYS205
CASP306

site_idAC7
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CL C1332
ChainResidue
CARG166
CARG252
CHIS256
DASP73
DHOH2058

site_idAC8
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CL D1331
ChainResidue
CASP73
DARG166
DARG252
DHIS256
DHOH2208

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsActive site: {"description":"Proton acceptor","evidences":[{"source":"UniProtKB","id":"P61889","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues40
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"12581646","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues14
DetailsBinding site: {"evidences":[{"source":"UniProtKB","id":"P61889","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 1emd
ChainResidueDetails
AHIS195
AASP168

site_idCSA2
Number of Residues2
DetailsAnnotated By Reference To The Literature 1emd
ChainResidueDetails
BHIS195
BASP168

site_idCSA3
Number of Residues2
DetailsAnnotated By Reference To The Literature 1emd
ChainResidueDetails
CHIS195
CASP168

site_idCSA4
Number of Residues2
DetailsAnnotated By Reference To The Literature 1emd
ChainResidueDetails
DHIS195
DASP168

site_idCSA5
Number of Residues3
DetailsAnnotated By Reference To The Literature 1emd
ChainResidueDetails
AHIS195
AARG171
AASP168

site_idCSA6
Number of Residues3
DetailsAnnotated By Reference To The Literature 1emd
ChainResidueDetails
BHIS195
BARG171
BASP168

site_idCSA7
Number of Residues3
DetailsAnnotated By Reference To The Literature 1emd
ChainResidueDetails
CHIS195
CARG171
CASP168

site_idCSA8
Number of Residues3
DetailsAnnotated By Reference To The Literature 1emd
ChainResidueDetails
DHIS195
DARG171
DASP168

239803

PDB entries from 2025-08-06

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