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1UXH

Large improvement in the thermal stability of a tetrameric malate dehydrogenase by single point mutations at the dimer-dimer interface

Functional Information from GO Data
ChainGOidnamespacecontents
A0003824molecular_functioncatalytic activity
A0005737cellular_componentcytoplasm
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
B0005737cellular_componentcytoplasm
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
Functional Information from PDB Data
site_idAC1
Number of Residues31
DetailsBINDING SITE FOR RESIDUE NAD A 1310
ChainResidue
AGLY11
AGLY79
AALA80
APRO81
AASN95
ACYS102
AVAL118
AASN120
ALEU122
AGLN143
ALEU147
APHE12
AHIS175
APRO229
AFUM1311
AHOH2233
AHOH2234
AHOH2235
AHOH2236
AHOH2237
AHOH2238
AHOH2239
AVAL13
AHOH2240
AHOH2241
AASP33
AILE34
AVAL35
ATYR65
ATHR77
ASER78

site_idAC2
Number of Residues11
DetailsBINDING SITE FOR RESIDUE FUM A 1311
ChainResidue
AARG82
AARG88
AASN120
ALEU147
AARG151
AHIS175
AGLY213
ASER224
ANAD1310
AHOH2154
AHOH2240

site_idAC3
Number of Residues32
DetailsBINDING SITE FOR RESIDUE NAD B 1310
ChainResidue
BGLY9
BGLY11
BPHE12
BVAL13
BLEU32
BASP33
BILE34
BVAL35
BTYR65
BTHR77
BSER78
BGLY79
BALA80
BPRO81
BASN95
BCYS102
BVAL118
BASN120
BLEU122
BGLN143
BLEU147
BHIS175
BPRO229
BFUM1311
BHOH2011
BHOH2154
BHOH2205
BHOH2206
BHOH2207
BHOH2208
BHOH2209
BHOH2211

site_idAC4
Number of Residues10
DetailsBINDING SITE FOR RESIDUE FUM B 1311
ChainResidue
BARG82
BARG88
BASN120
BLEU147
BARG151
BHIS175
BGLY213
BSER224
BNAD1310
BHOH2211

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Proton acceptor => ECO:0000250|UniProtKB:P61889, ECO:0000255|HAMAP-Rule:MF_00487
ChainResidueDetails
AHIS175
BHIS175

site_idSWS_FT_FI2
Number of Residues6
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00487, ECO:0000269|PubMed:12054817, ECO:0000269|PubMed:14636605
ChainResidueDetails
AGLY9
AASP33
AVAL118
BGLY9
BASP33
BVAL118

site_idSWS_FT_FI3
Number of Residues10
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:P61889, ECO:0000255|HAMAP-Rule:MF_00487
ChainResidueDetails
AARG82
BARG151
AARG88
AASN95
AASN120
AARG151
BARG82
BARG88
BASN95
BASN120

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 1emd
ChainResidueDetails
AHIS175
AASP148

site_idCSA2
Number of Residues2
DetailsAnnotated By Reference To The Literature 1emd
ChainResidueDetails
BHIS175
BASP148

site_idCSA3
Number of Residues3
DetailsAnnotated By Reference To The Literature 1emd
ChainResidueDetails
AHIS175
AASP148
AARG151

site_idCSA4
Number of Residues3
DetailsAnnotated By Reference To The Literature 1emd
ChainResidueDetails
BHIS175
BASP148
BARG151

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PDB entries from 2024-10-30

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