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2E37

Structure of TT0471 protein from Thermus thermophilus

Functional Information from GO Data
ChainGOidnamespacecontents
A0003824molecular_functioncatalytic activity
A0004459molecular_functionL-lactate dehydrogenase activity
A0005737cellular_componentcytoplasm
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
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
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
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
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
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
G0003824molecular_functioncatalytic activity
G0004459molecular_functionL-lactate dehydrogenase activity
G0005737cellular_componentcytoplasm
G0006096biological_processglycolytic process
G0016491molecular_functionoxidoreductase activity
G0016616molecular_functionoxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
G0019752biological_processcarboxylic acid metabolic process
H0003824molecular_functioncatalytic activity
H0004459molecular_functionL-lactate dehydrogenase activity
H0005737cellular_componentcytoplasm
H0006096biological_processglycolytic process
H0016491molecular_functionoxidoreductase activity
H0016616molecular_functionoxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
H0019752biological_processcarboxylic acid metabolic process
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 B 1501
ChainResidue
BVAL6
BGLY7
BASP32
BLEU33

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 H 1502
ChainResidue
HASP32
HLEU33
HTYR62
HALA75

site_idAC3
Number of Residues18
DetailsBINDING SITE FOR RESIDUE NAD A 1401
ChainResidue
AGLY9
AMSE10
AVAL11
AASP32
ALEU33
ALEU37
AALA74
AALA75
AGLY76
AVAL77
AASN92
ATHR116
AASN117
AILE221
AALA226
ATHR227
AHOH1411
ASER8

site_idAC4
Number of Residues18
DetailsBINDING SITE FOR RESIDUE NAD C 1402
ChainResidue
CGLY7
CSER8
CGLY9
CMSE10
CVAL11
CASP32
CLEU33
CLEU37
CALA75
CGLY76
CVAL77
CASN92
CVAL95
CASN117
CILE221
CALA226
CTHR227
CHOH1479

site_idAC5
Number of Residues16
DetailsBINDING SITE FOR RESIDUE NAD E 1403
ChainResidue
ESER8
EGLY9
EMSE10
EVAL11
EASP32
ELEU33
ELEU37
EALA75
EGLY76
EVAL77
EASN92
EASN117
EILE221
EALA226
ETHR227
EHOH1410

site_idAC6
Number of Residues18
DetailsBINDING SITE FOR RESIDUE NAD G 1404
ChainResidue
GSER8
GGLY9
GMSE10
GVAL11
GASP32
GLEU33
GLEU37
GALA75
GGLY76
GVAL77
GASN92
GVAL95
GASN117
GILE221
GALA226
GTHR227
GHOH1437
GHOH1480

Functional Information from PROSITE/UniProt
site_idPS00064
Number of Residues7
DetailsL_LDH L-lactate dehydrogenase active site. LGEHGDS
ChainResidueDetails
ALEU169-SER175

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues8
DetailsACT_SITE: Proton acceptor => ECO:0000255|HAMAP-Rule:MF_00488, ECO:0000305|PubMed:17936781, ECO:0000305|Ref.4, ECO:0007744|PDB:2V7P, ECO:0007744|PDB:2XXJ
ChainResidueDetails
AHIS172
BHIS172
CHIS172
DHIS172
EHIS172
FHIS172
GHIS172
HHIS172

site_idSWS_FT_FI2
Number of Residues24
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00488, ECO:0000269|PubMed:17936781, ECO:0000269|Ref.2, ECO:0000269|Ref.4, ECO:0000305|PubMed:22319152, ECO:0007744|PDB:2E37, ECO:0007744|PDB:2V7P, ECO:0007744|PDB:2XXB, ECO:0007744|PDB:2XXJ, ECO:0007744|PDB:3ZZN
ChainResidueDetails
AMSE10
DMSE10
DASP32
DGLY76
EMSE10
EASP32
EGLY76
FMSE10
FASP32
FGLY76
GMSE10
AASP32
GASP32
GGLY76
HMSE10
HASP32
HGLY76
AGLY76
BMSE10
BASP32
BGLY76
CMSE10
CASP32
CGLY76

site_idSWS_FT_FI3
Number of Residues8
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00488, ECO:0000269|PubMed:17936781, ECO:0000269|Ref.4, ECO:0007744|PDB:2V7P, ECO:0007744|PDB:2XXB, ECO:0007744|PDB:2XXJ
ChainResidueDetails
ATYR62
BTYR62
CTYR62
DTYR62
ETYR62
FTYR62
GTYR62
HTYR62

site_idSWS_FT_FI4
Number of Residues16
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00488, ECO:0000305|PubMed:17936781, ECO:0000305|Ref.4, ECO:0007744|PDB:2V7P, ECO:0007744|PDB:2XXJ
ChainResidueDetails
AGLN79
EASP145
FGLN79
FASP145
GGLN79
GASP145
HGLN79
HASP145
AASP145
BGLN79
BASP145
CGLN79
CASP145
DGLN79
DASP145
EGLN79

site_idSWS_FT_FI5
Number of Residues16
DetailsBINDING: BINDING => ECO:0000305|PubMed:17936781, ECO:0000305|Ref.4, ECO:0007744|PDB:2V7P, ECO:0007744|PDB:2XXJ
ChainResidueDetails
AARG85
ETHR227
FARG85
FTHR227
GARG85
GTHR227
HARG85
HTHR227
ATHR227
BARG85
BTHR227
CARG85
CTHR227
DARG85
DTHR227
EARG85

site_idSWS_FT_FI6
Number of Residues8
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00488, ECO:0000269|PubMed:17936781, ECO:0000269|Ref.4, ECO:0007744|PDB:2V7P, ECO:0007744|PDB:2XXJ
ChainResidueDetails
AALA115
BALA115
CALA115
DALA115
EALA115
FALA115
GALA115
HALA115

site_idSWS_FT_FI7
Number of Residues24
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00488
ChainResidueDetails
AASN117
DASN117
DARG150
DHIS165
EASN117
EARG150
EHIS165
FASN117
FARG150
FHIS165
GASN117
AARG150
GARG150
GHIS165
HASN117
HARG150
HHIS165
AHIS165
BASN117
BARG150
BHIS165
CASN117
CARG150
CHIS165

site_idSWS_FT_FI8
Number of Residues8
DetailsBINDING: BINDING => ECO:0000269|PubMed:17936781, ECO:0000269|Ref.4, ECO:0007744|PDB:2V7P, ECO:0007744|PDB:2XXJ
ChainResidueDetails
ASER140
BSER140
CSER140
DSER140
ESER140
FSER140
GSER140
HSER140

site_idSWS_FT_FI9
Number of Residues8
DetailsMOD_RES: Phosphotyrosine => ECO:0000255|HAMAP-Rule:MF_00488
ChainResidueDetails
ATYR218
BTYR218
CTYR218
DTYR218
ETYR218
FTYR218
GTYR218
HTYR218

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 1emd
ChainResidueDetails
AHIS172
AASP145

site_idCSA10
Number of Residues3
DetailsAnnotated By Reference To The Literature 1emd
ChainResidueDetails
BHIS172
BASP145
BARG148

site_idCSA11
Number of Residues3
DetailsAnnotated By Reference To The Literature 1emd
ChainResidueDetails
CHIS172
CASP145
CARG148

site_idCSA12
Number of Residues3
DetailsAnnotated By Reference To The Literature 1emd
ChainResidueDetails
DHIS172
DASP145
DARG148

site_idCSA13
Number of Residues3
DetailsAnnotated By Reference To The Literature 1emd
ChainResidueDetails
EHIS172
EASP145
EARG148

site_idCSA14
Number of Residues3
DetailsAnnotated By Reference To The Literature 1emd
ChainResidueDetails
FHIS172
FASP145
FARG148

site_idCSA15
Number of Residues3
DetailsAnnotated By Reference To The Literature 1emd
ChainResidueDetails
GHIS172
GASP145
GARG148

site_idCSA16
Number of Residues3
DetailsAnnotated By Reference To The Literature 1emd
ChainResidueDetails
HHIS172
HASP145
HARG148

site_idCSA2
Number of Residues2
DetailsAnnotated By Reference To The Literature 1emd
ChainResidueDetails
BHIS172
BASP145

site_idCSA3
Number of Residues2
DetailsAnnotated By Reference To The Literature 1emd
ChainResidueDetails
CHIS172
CASP145

site_idCSA4
Number of Residues2
DetailsAnnotated By Reference To The Literature 1emd
ChainResidueDetails
DHIS172
DASP145

site_idCSA5
Number of Residues2
DetailsAnnotated By Reference To The Literature 1emd
ChainResidueDetails
EHIS172
EASP145

site_idCSA6
Number of Residues2
DetailsAnnotated By Reference To The Literature 1emd
ChainResidueDetails
FHIS172
FASP145

site_idCSA7
Number of Residues2
DetailsAnnotated By Reference To The Literature 1emd
ChainResidueDetails
GHIS172
GASP145

site_idCSA8
Number of Residues2
DetailsAnnotated By Reference To The Literature 1emd
ChainResidueDetails
HHIS172
HASP145

site_idCSA9
Number of Residues3
DetailsAnnotated By Reference To The Literature 1emd
ChainResidueDetails
AHIS172
AASP145
AARG148

223532

PDB entries from 2024-08-07

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