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6JML

Re-refined structure of R-state L-lactate dehydrogenase fromLactobacillus casei

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
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
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
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
E0003824molecular_functioncatalytic activity
E0004459molecular_functionL-lactate dehydrogenase activity
E0005737cellular_componentcytoplasm
E0006089biological_processlactate metabolic process
E0006090biological_processpyruvate metabolic process
E0006096biological_processglycolytic process
E0016491molecular_functionoxidoreductase activity
E0016616molecular_functionoxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
E0019752biological_processcarboxylic acid metabolic process
F0003824molecular_functioncatalytic activity
F0004459molecular_functionL-lactate dehydrogenase activity
F0005737cellular_componentcytoplasm
F0006089biological_processlactate metabolic process
F0006090biological_processpyruvate metabolic process
F0006096biological_processglycolytic process
F0016491molecular_functionoxidoreductase activity
F0016616molecular_functionoxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
F0019752biological_processcarboxylic acid metabolic process
Functional Information from PDB Data
site_idAC1
Number of Residues6
Detailsbinding site for residue SO4 A 401
ChainResidue
ALEU153
AARG157
AHIS181
AALA225
ATHR235
AHOH502

site_idAC2
Number of Residues10
Detailsbinding site for residue SO4 A 402
ChainResidue
AHOH505
AHOH520
BSER172
BHIS174
BGLY195
BHOH509
BHOH530
AARG159
AHIS174
ATYR176

site_idAC3
Number of Residues7
Detailsbinding site for residue SO4 B 401
ChainResidue
BLEU153
BARG157
BHIS181
BALA225
BTHR235
BHOH523
BHOH527

site_idAC4
Number of Residues9
Detailsbinding site for residue SO4 B 402
ChainResidue
ASER172
AHIS174
AGLY195
AHOH539
BARG159
BHIS174
BTYR176
BHOH520
BHOH536

site_idAC5
Number of Residues5
Detailsbinding site for residue SO4 C 401
ChainResidue
CLEU153
CARG157
CHIS181
CALA225
CTHR235

site_idAC6
Number of Residues10
Detailsbinding site for residue SO4 C 402
ChainResidue
CARG159
CHIS174
CTYR176
CHOH503
CHOH509
CHOH524
CHOH530
FSER172
FHIS174
FGLY195

site_idAC7
Number of Residues5
Detailsbinding site for residue SO4 D 401
ChainResidue
DLEU153
DARG157
DHIS181
DALA225
DTHR235

site_idAC8
Number of Residues6
Detailsbinding site for residue SO4 D 402
ChainResidue
DARG159
DHIS174
DTYR176
DHOH501
EHIS174
EHOH509

site_idAC9
Number of Residues6
Detailsbinding site for residue SO4 E 401
ChainResidue
EASN126
ELEU153
EARG157
EHIS181
EALA225
ETHR235

site_idAD1
Number of Residues10
Detailsbinding site for residue SO4 E 402
ChainResidue
DSER172
DHIS174
DGLY195
DHOH503
EARG159
EHIS174
ETYR176
EHOH504
EHOH507
EHOH508

site_idAD2
Number of Residues7
Detailsbinding site for residue SO4 F 401
ChainResidue
FLEU153
FARG157
FHIS181
FALA225
FTHR235
FHOH501
FHOH504

site_idAD3
Number of Residues9
Detailsbinding site for residue SO4 F 402
ChainResidue
CHIS174
CGLY195
CHOH502
FARG159
FHIS174
FTYR176
FHOH506
FHOH509
FHOH518

Functional Information from PROSITE/UniProt
site_idPS00064
Number of Residues7
DetailsL_LDH L-lactate dehydrogenase active site. MGEHGDT
ChainResidueDetails
AMET178-THR184

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues6
DetailsACT_SITE: Proton acceptor => ECO:0000255|HAMAP-Rule:MF_00488, ECO:0000305|Ref.6, ECO:0000305|Ref.8, ECO:0007744|PDB:1LLC, ECO:0007744|PDB:6J9T, ECO:0007744|PDB:6J9U
ChainResidueDetails
AHIS181
BHIS181
CHIS181
DHIS181
EHIS181
FHIS181

site_idSWS_FT_FI2
Number of Residues60
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00488
ChainResidueDetails
AVAL20
AHIS174
BVAL20
BASP41
BLYS46
BTYR71
BGLY85
BGLN88
BSER107
BALA124
BSER149
AASP41
BHIS174
CVAL20
CASP41
CLYS46
CTYR71
CGLY85
CGLN88
CSER107
CALA124
CSER149
ALYS46
CHIS174
DVAL20
DASP41
DLYS46
DTYR71
DGLY85
DGLN88
DSER107
DALA124
DSER149
ATYR71
DHIS174
EVAL20
EASP41
ELYS46
ETYR71
EGLY85
EGLN88
ESER107
EALA124
ESER149
AGLY85
EHIS174
FVAL20
FASP41
FLYS46
FTYR71
FGLY85
FGLN88
FSER107
FALA124
FSER149
AGLN88
FHIS174
ASER107
AALA124
ASER149

site_idSWS_FT_FI3
Number of Residues6
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00488, ECO:0000269|Ref.8, ECO:0007744|PDB:6J9U
ChainResidueDetails
AARG94
BARG94
CARG94
DARG94
EARG94
FARG94

site_idSWS_FT_FI4
Number of Residues6
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00488, ECO:0000305|Ref.8, ECO:0007744|PDB:6J9U
ChainResidueDetails
AASN126
BASN126
CASN126
DASN126
EASN126
FASN126

site_idSWS_FT_FI5
Number of Residues6
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00488, ECO:0000305|Ref.8, ECO:0007744|PDB:6J9S, ECO:0007744|PDB:6J9T, ECO:0007744|PDB:6J9U
ChainResidueDetails
AASP154
BASP154
CASP154
DASP154
EASP154
FASP154

site_idSWS_FT_FI6
Number of Residues6
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00488, ECO:0000269|Ref.8, ECO:0007744|PDB:6J9T, ECO:0007744|PDB:6J9U
ChainResidueDetails
AARG159
BARG159
CARG159
DARG159
EARG159
FARG159

site_idSWS_FT_FI7
Number of Residues6
DetailsBINDING: BINDING => ECO:0000269|Ref.8, ECO:0007744|PDB:6J9T
ChainResidueDetails
AARG171
BARG171
CARG171
DARG171
EARG171
FARG171

site_idSWS_FT_FI8
Number of Residues6
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00488, ECO:0000269|Ref.8, ECO:0007744|PDB:6J9S, ECO:0007744|PDB:6J9U
ChainResidueDetails
ATHR235
BTHR235
CTHR235
DTHR235
ETHR235
FTHR235

site_idSWS_FT_FI9
Number of Residues6
DetailsMOD_RES: Phosphotyrosine => ECO:0000255|HAMAP-Rule:MF_00488
ChainResidueDetails
ATYR226
BTYR226
CTYR226
DTYR226
ETYR226
FTYR226

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PDB entries from 2024-07-31

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