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2LDB

STRUCTURE DETERMINATION AND REFINEMENT OF BACILLUS STEAROTHERMOPHILUS LACTATE DEHYDROGENASE

Functional Information from GO Data
ChainGOidnamespacecontents
A0003824molecular_functioncatalytic activity
A0004459molecular_functionL-lactate dehydrogenase activity
A0005737cellular_componentcytoplasm
A0006089biological_processlactate metabolic process
A0006090biological_processpyruvate metabolic process
A0006096biological_processglycolytic process
A0016491molecular_functionoxidoreductase activity
A0016616molecular_functionoxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
A0019752biological_processcarboxylic acid metabolic process
A0051287molecular_functionNAD binding
B0003824molecular_functioncatalytic activity
B0004459molecular_functionL-lactate dehydrogenase activity
B0005737cellular_componentcytoplasm
B0006089biological_processlactate metabolic process
B0006090biological_processpyruvate metabolic process
B0006096biological_processglycolytic process
B0016491molecular_functionoxidoreductase activity
B0016616molecular_functionoxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
B0019752biological_processcarboxylic acid metabolic process
B0051287molecular_functionNAD binding
C0003824molecular_functioncatalytic activity
C0004459molecular_functionL-lactate dehydrogenase activity
C0005737cellular_componentcytoplasm
C0006089biological_processlactate metabolic process
C0006090biological_processpyruvate metabolic process
C0006096biological_processglycolytic process
C0016491molecular_functionoxidoreductase activity
C0016616molecular_functionoxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
C0019752biological_processcarboxylic acid metabolic process
C0051287molecular_functionNAD binding
D0003824molecular_functioncatalytic activity
D0004459molecular_functionL-lactate dehydrogenase activity
D0005737cellular_componentcytoplasm
D0006089biological_processlactate metabolic process
D0006090biological_processpyruvate metabolic process
D0006096biological_processglycolytic process
D0016491molecular_functionoxidoreductase activity
D0016616molecular_functionoxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
D0019752biological_processcarboxylic acid metabolic process
D0051287molecular_functionNAD binding
Functional Information from PDB Data
site_idFBA
Number of Residues10
DetailsFBP binding site
ChainResidue
AARG171
APRO182
AGLN183
AASN184
AVAL185
AHIS186
AALA187
ATYR188
AGLY207
AILE269

site_idFBB
Number of Residues10
DetailsFBP binding site
ChainResidue
BARG171
BPRO182
BGLN183
BASN184
BVAL185
BHIS186
BALA187
BTYR188
BGLY207
BILE269

site_idFBC
Number of Residues10
DetailsFBP binding site
ChainResidue
CVAL185
CHIS186
CALA187
CTYR188
CGLY207
CILE269
CARG171
CPRO182
CGLN183
CASN184

site_idFBD
Number of Residues10
DetailsFBP binding site
ChainResidue
DARG171
DPRO182
DGLN183
DASN184
DVAL185
DHIS186
DALA187
DTYR188
DGLY207
DILE269

site_idNAA
Number of Residues25
DetailsNAD binding site
ChainResidue
AILE26
AALA53
AASN54
ALYS57
ATYR83
ACYS95
AALA96
AGLY97
AALA98
AILE116
AILE120
AGLY27
AALA136
ATHR137
AASN138
ASER161
ALEU165
AHIS193
AALA28
AGLY29
APHE30
AVAL31
AGLY32
AILE51
AASP52

site_idNAB
Number of Residues25
DetailsNAD binding site
ChainResidue
BILE26
BGLY27
BALA28
BGLY29
BPHE30
BVAL31
BGLY32
BILE51
BASP52
BALA53
BASN54
BLYS57
BTYR83
BCYS95
BALA96
BGLY97
BALA98
BILE116
BILE120
BALA136
BTHR137
BASN138
BSER161
BLEU165
BHIS193

site_idNAC
Number of Residues25
DetailsNAD binding site
ChainResidue
CILE26
CGLY27
CALA28
CGLY29
CPHE30
CVAL31
CGLY32
CILE51
CASP52
CALA53
CASN54
CLYS57
CTYR83
CCYS95
CALA96
CGLY97
CALA98
CILE116
CILE120
CALA136
CTHR137
CASN138
CSER161
CLEU165
CHIS193

site_idNAD
Number of Residues25
DetailsNAD binding site
ChainResidue
DILE26
DGLY27
DALA28
DGLY29
DPHE30
DVAL31
DGLY32
DILE51
DASP52
DALA53
DASN54
DLYS57
DTYR83
DCYS95
DALA96
DGLY97
DALA98
DILE116
DILE120
DALA136
DTHR137
DASN138
DSER161
DLEU165
DHIS193

Functional Information from PROSITE/UniProt
site_idPS00064
Number of Residues7
DetailsL_LDH L-lactate dehydrogenase active site. IGEHGDT
ChainResidueDetails
AILE190-THR196

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsACT_SITE: Proton acceptor => ECO:0000255|HAMAP-Rule:MF_00488, ECO:0000305|PubMed:1731077, ECO:0007744|PDB:1LDN
ChainResidueDetails
AHIS193
BHIS193
CHIS193
DHIS193

site_idSWS_FT_FI2
Number of Residues12
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00488, ECO:0000269|PubMed:1731077, ECO:0000269|PubMed:2330370, ECO:0007744|PDB:1LDN, ECO:0007744|PDB:2LDB
ChainResidueDetails
APHE30
DPHE30
DASP52
DALA136
AASP52
AALA136
BPHE30
BASP52
BALA136
CPHE30
CASP52
CALA136

site_idSWS_FT_FI3
Number of Residues24
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00488
ChainResidueDetails
ALYS57
BGLN100
BSER119
BASN138
CLYS57
CTYR83
CGLY97
CGLN100
CSER119
CASN138
DLYS57
ATYR83
DTYR83
DGLY97
DGLN100
DSER119
DASN138
AGLY97
AGLN100
ASER119
AASN138
BLYS57
BTYR83
BGLY97

site_idSWS_FT_FI4
Number of Residues12
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00488, ECO:0000305|PubMed:1731077, ECO:0007744|PDB:1LDN
ChainResidueDetails
AARG106
DARG106
DASP166
DTHR247
AASP166
ATHR247
BARG106
BASP166
BTHR247
CARG106
CASP166
CTHR247

site_idSWS_FT_FI5
Number of Residues8
DetailsBINDING: BINDING => ECO:0000269|PubMed:1731077, ECO:0000269|PubMed:2330370, ECO:0007744|PDB:1LDN, ECO:0007744|PDB:2LDB
ChainResidueDetails
ASER161
AGLN183
BSER161
BGLN183
CSER161
CGLN183
DSER161
DGLN183

site_idSWS_FT_FI6
Number of Residues4
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00488, ECO:0000269|PubMed:2330370, ECO:0007744|PDB:2LDB
ChainResidueDetails
AARG171
BARG171
CARG171
DARG171

site_idSWS_FT_FI7
Number of Residues4
DetailsMOD_RES: Phosphotyrosine => ECO:0000255|HAMAP-Rule:MF_00488
ChainResidueDetails
ATYR238
BTYR238
CTYR238
DTYR238

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 1emd
ChainResidueDetails
AASP166
AHIS193

site_idCSA2
Number of Residues2
DetailsAnnotated By Reference To The Literature 1emd
ChainResidueDetails
BASP166
BHIS193

site_idCSA3
Number of Residues2
DetailsAnnotated By Reference To The Literature 1emd
ChainResidueDetails
CASP166
CHIS193

site_idCSA4
Number of Residues2
DetailsAnnotated By Reference To The Literature 1emd
ChainResidueDetails
DASP166
DHIS193

site_idCSA5
Number of Residues3
DetailsAnnotated By Reference To The Literature 1emd
ChainResidueDetails
AHIS193
AASP166
AARG169

site_idCSA6
Number of Residues3
DetailsAnnotated By Reference To The Literature 1emd
ChainResidueDetails
BHIS193
BASP166
BARG169

site_idCSA7
Number of Residues3
DetailsAnnotated By Reference To The Literature 1emd
ChainResidueDetails
CHIS193
CASP166
CARG169

site_idCSA8
Number of Residues3
DetailsAnnotated By Reference To The Literature 1emd
ChainResidueDetails
DHIS193
DASP166
DARG169

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PDB entries from 2024-11-06

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