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6RJB

Human transketolase variant T382E

Functional Information from GO Data
ChainGOidnamespacecontents
A0000287molecular_functionmagnesium ion binding
A0003824molecular_functioncatalytic activity
A0004802molecular_functiontransketolase activity
A0005509molecular_functioncalcium ion binding
A0005515molecular_functionprotein binding
A0005654cellular_componentnucleoplasm
A0005737cellular_componentcytoplasm
A0005777cellular_componentperoxisome
A0005789cellular_componentendoplasmic reticulum membrane
A0005829cellular_componentcytosol
A0006098biological_processpentose-phosphate shunt
A0009052biological_processpentose-phosphate shunt, non-oxidative branch
A0016604cellular_componentnuclear body
A0016740molecular_functiontransferase activity
A0030976molecular_functionthiamine pyrophosphate binding
A0031982cellular_componentvesicle
A0040008biological_processregulation of growth
A0042803molecular_functionprotein homodimerization activity
A0046166biological_processglyceraldehyde-3-phosphate biosynthetic process
A0046872molecular_functionmetal ion binding
A0070062cellular_componentextracellular exosome
A1901159biological_processxylulose 5-phosphate biosynthetic process
B0000287molecular_functionmagnesium ion binding
B0003824molecular_functioncatalytic activity
B0004802molecular_functiontransketolase activity
B0005509molecular_functioncalcium ion binding
B0005515molecular_functionprotein binding
B0005654cellular_componentnucleoplasm
B0005737cellular_componentcytoplasm
B0005777cellular_componentperoxisome
B0005789cellular_componentendoplasmic reticulum membrane
B0005829cellular_componentcytosol
B0006098biological_processpentose-phosphate shunt
B0009052biological_processpentose-phosphate shunt, non-oxidative branch
B0016604cellular_componentnuclear body
B0016740molecular_functiontransferase activity
B0030976molecular_functionthiamine pyrophosphate binding
B0031982cellular_componentvesicle
B0040008biological_processregulation of growth
B0042803molecular_functionprotein homodimerization activity
B0046166biological_processglyceraldehyde-3-phosphate biosynthetic process
B0046872molecular_functionmetal ion binding
B0070062cellular_componentextracellular exosome
B1901159biological_processxylulose 5-phosphate biosynthetic process
Functional Information from PDB Data
site_idAC1
Number of Residues27
Detailsbinding site for residue TPP A 701
ChainResidue
ASER40
AGLU157
AGLU160
AASN185
ALEU187
AGLY188
AGLN189
ALYS244
AHIS258
AMG702
ACA703
ALYS75
AHOH964
AHOH1288
BASP341
BILE364
BGLU366
BPHE392
BARG395
BGLN428
AHIS77
AGLY123
ASER124
ALEU125
AGLY154
AASP155
AGLY156

site_idAC2
Number of Residues5
Detailsbinding site for residue MG A 702
ChainResidue
AASP155
AASN185
ALEU187
ATPP701
AHOH964

site_idAC3
Number of Residues5
Detailsbinding site for residue CA A 703
ChainResidue
AASP155
AASN185
ALEU187
ATPP701
AHOH964

site_idAC4
Number of Residues10
Detailsbinding site for residue GOL A 704
ChainResidue
APRO475
AASN477
AVAL510
APRO598
ALEU602
AHOH960
AHOH1125
AHOH1188
AHOH1295
AHOH1382

site_idAC5
Number of Residues7
Detailsbinding site for residue EDO A 705
ChainResidue
APRO63
AASN68
AASP69
AARG70
APHE71
AARG379
AHOH855

site_idAC6
Number of Residues8
Detailsbinding site for residue EDO A 706
ChainResidue
APHE71
AVAL72
ALEU73
ALEU82
APHE117
AHOH857
AHOH1040
AHOH1171

site_idAC7
Number of Residues11
Detailsbinding site for residue EDO A 707
ChainResidue
ALEU158
ASER159
ATRP164
ALEU195
AARG205
AEDO711
AHOH977
AHOH985
BPHE209
BPEG725
BHOH920

site_idAC8
Number of Residues7
Detailsbinding site for residue EDO A 708
ChainResidue
ATYR564
AALA588
AASN590
AHOH867
AHOH1013
AHOH1128
AHOH1221

site_idAC9
Number of Residues7
Detailsbinding site for residue EDO A 709
ChainResidue
AGLN189
ASER256
ATRP257
AHIS258
AHOH1065
AHOH1166
BASN344

site_idAD1
Number of Residues8
Detailsbinding site for residue EDO A 710
ChainResidue
ATYR563
ATYR564
AGLU565
AVAL589
AASN590
AHOH1206
BPRO441
BLYS538

site_idAD2
Number of Residues8
Detailsbinding site for residue EDO A 711
ChainResidue
BTRP164
BGLU165
BPHE209
BPEG725
ALEU158
ASER159
ATRP164
AEDO707

site_idAD3
Number of Residues6
Detailsbinding site for residue EDO A 712
ChainResidue
AARG21
AALA84
AGLU88
AGLU94
ALEU97
AHOH1256

site_idAD4
Number of Residues9
Detailsbinding site for residue EDO A 713
ChainResidue
AVAL120
AGLN127
AALA131
ASER371
AVAL374
AGLN399
AMET402
AALA403
AHOH823

site_idAD5
Number of Residues7
Detailsbinding site for residue EDO A 714
ChainResidue
AGLU423
ALYS597
AHOH840
AHOH884
AHOH1234
BALA33
BARG101

site_idAD6
Number of Residues8
Detailsbinding site for residue EDO A 715
ChainResidue
ALEU92
AASP106
ALEU107
AGLN115
AEDO719
AHOH875
AHOH890
AHOH899

site_idAD7
Number of Residues6
Detailsbinding site for residue EDO A 716
ChainResidue
ATYR137
ATYR173
AHOH929
AHOH1088
AHOH1091
AHOH1212

site_idAD8
Number of Residues5
Detailsbinding site for residue EDO A 717
ChainResidue
AALA326
ALYS327
AHIS330
AGLU354
AHOH917

site_idAD9
Number of Residues7
Detailsbinding site for residue EDO A 718
ChainResidue
APRO307
ASER308
ATYR309
ALYS327
AGLU455
AHOH828
AHOH833

site_idAE1
Number of Residues5
Detailsbinding site for residue EDO A 719
ChainResidue
APHE91
ALEU92
AEDO715
AHOH1012
AHOH1059

site_idAE2
Number of Residues3
Detailsbinding site for residue EDO A 720
ChainResidue
AASP217
AHOH856
AHOH1034

site_idAE3
Number of Residues3
Detailsbinding site for residue EDO A 721
ChainResidue
AASP217
AHIS219
ALYS241

site_idAE4
Number of Residues5
Detailsbinding site for residue EDO A 722
ChainResidue
AARG246
AGLY247
AGLU252
AHOH845
AHOH967

site_idAE5
Number of Residues5
Detailsbinding site for residue EDO A 723
ChainResidue
AALA462
AASN463
ATHR464
ALYS465
AHOH939

site_idAE6
Number of Residues5
Detailsbinding site for residue EDO A 724
ChainResidue
AARG318
ASER345
AHIS416
AARG474
AHOH1047

site_idAE7
Number of Residues6
Detailsbinding site for residue NA A 725
ChainResidue
AASN411
AALA461
ATHR464
ACYS468
AHOH844
AHOH1143

site_idAE8
Number of Residues8
Detailsbinding site for residue NA A 726
ChainResidue
ASER74
ATHR122
ASER124
ALEU125
AGLY126
AGLN127
AGLY128
AGLU157

site_idAE9
Number of Residues10
Detailsbinding site for residue PEG A 727
ChainResidue
AGLU165
AALA168
APHE169
AILE172
ACYS362
AASN368
BSER159
BEDO705
BEDO708
BHOH1054

site_idAF1
Number of Residues27
Detailsbinding site for residue TPP B 701
ChainResidue
AASP341
AILE364
AGLU366
APHE392
AARG395
AGLN428
AHOH803
BSER40
BLYS75
BHIS77
BGLY123
BSER124
BLEU125
BGLY154
BASP155
BGLY156
BGLU157
BGLU160
BASN185
BLEU187
BGLY188
BGLN189
BLYS244
BHIS258
BMG702
BCA703
BHOH948

site_idAF2
Number of Residues5
Detailsbinding site for residue MG B 702
ChainResidue
BASP155
BASN185
BLEU187
BTPP701
BHOH948

site_idAF3
Number of Residues5
Detailsbinding site for residue CA B 703
ChainResidue
BASP155
BASN185
BLEU187
BTPP701
BHOH948

site_idAF4
Number of Residues7
Detailsbinding site for residue GOL B 704
ChainResidue
BARG318
BASN344
BSER345
BHIS416
BARG474
BHOH1019
BHOH1043

site_idAF5
Number of Residues12
Detailsbinding site for residue EDO B 705
ChainResidue
APHE209
APEG727
BLEU158
BSER159
BTRP164
BLEU195
BTYR202
BARG205
BEDO708
BHOH975
BHOH996
BHOH1054

site_idAF6
Number of Residues8
Detailsbinding site for residue EDO B 706
ChainResidue
BPHE71
BVAL72
BLEU73
BLEU82
BPHE117
BHOH818
BHOH1037
BHOH1135

site_idAF7
Number of Residues8
Detailsbinding site for residue EDO B 707
ChainResidue
APRO441
ALYS538
BTYR563
BTYR564
BGLU565
BVAL589
BASN590
BHOH1126

site_idAF8
Number of Residues7
Detailsbinding site for residue EDO B 708
ChainResidue
AGLU165
APHE209
APEG727
BLEU158
BSER159
BTRP164
BEDO705

site_idAF9
Number of Residues7
Detailsbinding site for residue EDO B 709
ChainResidue
AASN344
BGLN189
BSER256
BTRP257
BHIS258
BHOH1115
BHOH1145

site_idAG1
Number of Residues7
Detailsbinding site for residue EDO B 710
ChainResidue
AALA33
AARG101
ALYS102
BGLU423
BLYS597
BHOH860
BHOH998

site_idAG2
Number of Residues7
Detailsbinding site for residue EDO B 711
ChainResidue
BPRO63
BASN68
BASP69
BARG70
BPHE71
BARG379
BHOH872

site_idAG3
Number of Residues7
Detailsbinding site for residue EDO B 712
ChainResidue
BTYR564
BALA588
BASN590
BHOH856
BHOH935
BHOH1036
BHOH1156

site_idAG4
Number of Residues6
Detailsbinding site for residue EDO B 713
ChainResidue
BLEU92
BLEU107
BGLN115
BHOH857
BHOH914
BHOH924

site_idAG5
Number of Residues8
Detailsbinding site for residue EDO B 714
ChainResidue
BPRO475
BASN477
BVAL510
BPRO598
BHOH807
BHOH870
BHOH995
BHOH1171

site_idAG6
Number of Residues3
Detailsbinding site for residue EDO B 715
ChainResidue
BASN590
BARG591
BHOH838

site_idAG7
Number of Residues9
Detailsbinding site for residue EDO B 716
ChainResidue
BARG21
BSER25
BALA84
BALA87
BGLU88
BGLU94
BLEU97
BLYS283
BHOH843

site_idAG8
Number of Residues1
Detailsbinding site for residue EDO B 717
ChainResidue
BGLN10

site_idAG9
Number of Residues4
Detailsbinding site for residue EDO B 718
ChainResidue
BMET199
BASP217
BHOH811
BHOH1020

site_idAH1
Number of Residues8
Detailsbinding site for residue EDO B 719
ChainResidue
BALA316
BTHR317
BSER449
BSER473
BPRO475
BASN477
BGLY509
BVAL510

site_idAH2
Number of Residues4
Detailsbinding site for residue EDO B 720
ChainResidue
BALA267
BGLU268
BHOH951
BHOH1078

site_idAH3
Number of Residues7
Detailsbinding site for residue EDO B 721
ChainResidue
AARG205
AHOH1332
BALA168
BSER171
BILE172
BHOH920
BHOH1292

site_idAH4
Number of Residues5
Detailsbinding site for residue EDO B 722
ChainResidue
BASP217
BHIS219
BLYS241
BHOH811
BHOH909

site_idAH5
Number of Residues6
Detailsbinding site for residue EDO B 723
ChainResidue
BASN300
BILE301
BARG302
BLEU460
BASN463
BHOH825

site_idAH6
Number of Residues8
Detailsbinding site for residue EDO B 724
ChainResidue
BVAL120
BGLN127
BSER371
BVAL374
BGLN399
BMET402
BALA403
BHOH839

site_idAH7
Number of Residues11
Detailsbinding site for residue PEG B 725
ChainResidue
ASER159
AEDO707
AEDO711
BGLU165
BALA168
BPHE169
BILE172
BCYS362
BALA365
BASN368
BHOH920

Functional Information from PROSITE/UniProt
site_idPS00801
Number of Residues21
DetailsTRANSKETOLASE_1 Transketolase signature 1. RissIQattaagSGHPTscCS
ChainResidueDetails
AARG23-SER43

site_idPS00802
Number of Residues17
DetailsTRANSKETOLASE_2 Transketolase signature 2. GEDGPSQmALEdlAmfR
ChainResidueDetails
AGLY422-ARG438

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Proton donor => ECO:0000250
ChainResidueDetails
AGLU366
BGLU366

site_idSWS_FT_FI2
Number of Residues12
DetailsBINDING: BINDING => ECO:0000250
ChainResidueDetails
AHIS37
BHIS416
BASP424
BARG474
AARG318
ASER345
AHIS416
AASP424
AARG474
BHIS37
BARG318
BSER345

site_idSWS_FT_FI3
Number of Residues22
DetailsBINDING:
ChainResidueDetails
ASER40
APHE392
AGLN428
BSER40
BHIS77
BGLY123
BASP155
BGLY156
BASN185
BLEU187
BLYS244
AHIS77
BHIS258
BPHE392
BGLN428
AGLY123
AASP155
AGLY156
AASN185
ALEU187
ALYS244
AHIS258

site_idSWS_FT_FI4
Number of Residues4
DetailsSITE: Important for catalytic activity => ECO:0000250
ChainResidueDetails
AHIS37
AHIS258
BHIS37
BHIS258

site_idSWS_FT_FI5
Number of Residues2
DetailsMOD_RES: N-acetylmethionine => ECO:0007744|PubMed:22814378
ChainResidueDetails
AMET1
BMET1

site_idSWS_FT_FI6
Number of Residues4
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:23186163
ChainResidueDetails
ASER3
ASER104
BSER3
BSER104

site_idSWS_FT_FI7
Number of Residues14
DetailsMOD_RES: N6-acetyllysine => ECO:0007744|PubMed:19608861
ChainResidueDetails
ALYS6
BLYS144
BLYS204
BLYS241
BLYS260
BLYS603
ALYS11
ALYS144
ALYS204
ALYS241
ALYS260
ALYS603
BLYS6
BLYS11

site_idSWS_FT_FI8
Number of Residues4
DetailsMOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:P40142
ChainResidueDetails
ALYS232
ALYS538
BLYS232
BLYS538

site_idSWS_FT_FI9
Number of Residues2
DetailsMOD_RES: Phosphotyrosine => ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231
ChainResidueDetails
ATYR275
BTYR275

site_idSWS_FT_FI10
Number of Residues2
DetailsMOD_RES: Phosphothreonine => ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163
ChainResidueDetails
ATHR287
BTHR287

site_idSWS_FT_FI11
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163
ChainResidueDetails
ASER295
BSER295

site_idSWS_FT_FI12
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P50137
ChainResidueDetails
ASER345
BSER345

site_idSWS_FT_FI13
Number of Residues4
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) => ECO:0007744|PubMed:28112733
ChainResidueDetails
ALYS352
BLYS352

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PDB entries from 2024-07-24

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