Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

6UB9

Crystal structure of tryptophan synthase from M. tuberculosis - AMINOACRYLATE- AND BRD6309-BOUND FORM

Replaces:  6DUA
Functional Information from GO Data
ChainGOidnamespacecontents
A0000162biological_processtryptophan biosynthetic process
A0004834molecular_functiontryptophan synthase activity
A0005829cellular_componentcytosol
A0005886cellular_componentplasma membrane
A0006568biological_processtryptophan metabolic process
A0016829molecular_functionlyase activity
B0000162biological_processtryptophan biosynthetic process
B0004834molecular_functiontryptophan synthase activity
B0005737cellular_componentcytoplasm
B0006568biological_processtryptophan metabolic process
B0016829molecular_functionlyase activity
C0000162biological_processtryptophan biosynthetic process
C0004834molecular_functiontryptophan synthase activity
C0005829cellular_componentcytosol
C0005886cellular_componentplasma membrane
C0006568biological_processtryptophan metabolic process
C0016829molecular_functionlyase activity
D0000162biological_processtryptophan biosynthetic process
D0004834molecular_functiontryptophan synthase activity
D0005737cellular_componentcytoplasm
D0006568biological_processtryptophan metabolic process
D0016829molecular_functionlyase activity
E0000162biological_processtryptophan biosynthetic process
E0004834molecular_functiontryptophan synthase activity
E0005829cellular_componentcytosol
E0005886cellular_componentplasma membrane
E0006568biological_processtryptophan metabolic process
E0016829molecular_functionlyase activity
F0000162biological_processtryptophan biosynthetic process
F0004834molecular_functiontryptophan synthase activity
F0005737cellular_componentcytoplasm
F0006568biological_processtryptophan metabolic process
F0016829molecular_functionlyase activity
G0000162biological_processtryptophan biosynthetic process
G0004834molecular_functiontryptophan synthase activity
G0005829cellular_componentcytosol
G0005886cellular_componentplasma membrane
G0006568biological_processtryptophan metabolic process
G0016829molecular_functionlyase activity
H0000162biological_processtryptophan biosynthetic process
H0004834molecular_functiontryptophan synthase activity
H0005737cellular_componentcytoplasm
H0006568biological_processtryptophan metabolic process
H0016829molecular_functionlyase activity
Functional Information from PDB Data
site_idAC1
Number of Residues5
Detailsbinding site for residue FMT A 501
ChainResidue
AGLU57
AMET106
ATYR181
AILE237
AMLA502

site_idAC2
Number of Residues9
Detailsbinding site for residue MLA A 502
ChainResidue
AILE237
AVAL238
AGLY239
ASER240
AFMT501
ATYR181
AGLY217
ALEU218
AGLY219

site_idAC3
Number of Residues2
Detailsbinding site for residue FMT A 503
ChainResidue
AGLN144
BSER23

site_idAC4
Number of Residues18
Detailsbinding site for residue P1T B 501
ChainResidue
BHIS100
BLYS101
BTHR124
BGLY125
BALA126
BGLY127
BGLN128
BHIS129
BTHR204
BGLY246
BGLY247
BGLY248
BSER249
BASN250
BGLY317
BGLU364
BSER390
BHOH615

site_idAC5
Number of Residues14
Detailsbinding site for residue H9V B 502
ChainResidue
ATYR62
AASP64
AGLY66
AASP136
BLEU34
BILE184
BASN185
BPHE188
BTYR200
BPHE202
BPRO208
BPHE211
BPHE293
BHIS294

site_idAC6
Number of Residues5
Detailsbinding site for residue CS B 503
ChainResidue
BGLY246
BALA282
BTHR284
BTYR320
BGLY322

site_idAC7
Number of Residues2
Detailsbinding site for residue FMT B 504
ChainResidue
BGLU48
BARG114

site_idAC8
Number of Residues2
Detailsbinding site for residue FMT B 505
ChainResidue
BARG355
DLEU165

site_idAC9
Number of Residues2
Detailsbinding site for residue FMT B 506
ChainResidue
BPRO262
BARG265

site_idAD1
Number of Residues4
Detailsbinding site for residue ACT B 507
ChainResidue
BHIS312
BSER313
BASP319
BHOH633

site_idAD2
Number of Residues5
Detailsbinding site for residue FMT B 508
ChainResidue
BGLY67
BARG68
BPRO69
DGLY67
DPRO69

site_idAD3
Number of Residues6
Detailsbinding site for residue FMT B 509
ChainResidue
BLYS402
BTRP403
BHOH605
BHOH621
HLYS402
HTRP403

site_idAD4
Number of Residues5
Detailsbinding site for residue MLA C 501
ChainResidue
CTYR181
CGLY217
CGLY219
CGLY239
CSER240

site_idAD5
Number of Residues2
Detailsbinding site for residue FMT C 502
ChainResidue
CGLN144
DSER23

site_idAD6
Number of Residues20
Detailsbinding site for residue P1T D 501
ChainResidue
DSER390
DHOH610
DHIS100
DLYS101
DTHR124
DGLY125
DALA126
DGLY127
DGLN128
DHIS129
DTHR204
DCYS244
DGLY246
DGLY247
DGLY248
DSER249
DASN250
DGLY317
DLEU318
DGLU364

site_idAD7
Number of Residues14
Detailsbinding site for residue H9V D 502
ChainResidue
CTYR62
CASP64
CGLY66
CASP136
DVAL30
DPRO31
DLEU34
DILE184
DPHE188
DTYR200
DPHE202
DPRO208
DPHE211
DHIS294

site_idAD8
Number of Residues6
Detailsbinding site for residue CS D 503
ChainResidue
DGLY246
DALA282
DTHR284
DTYR320
DGLY322
DHOH613

site_idAD9
Number of Residues4
Detailsbinding site for residue PGE D 504
ChainResidue
DPRO262
DARG265
DGLY334
DARG335

site_idAE1
Number of Residues2
Detailsbinding site for residue FMT E 501
ChainResidue
EALA183
ESER184

site_idAE2
Number of Residues6
Detailsbinding site for residue MLA E 502
ChainResidue
ETYR181
EGLY217
EGLY219
EVAL238
EGLY239
ESER240

site_idAE3
Number of Residues19
Detailsbinding site for residue P1T F 501
ChainResidue
FHIS100
FLYS101
FTHR124
FGLY125
FALA126
FGLY127
FGLN128
FHIS129
FTHR204
FGLY246
FGLY247
FGLY248
FSER249
FASN250
FGLY317
FGLU364
FSER390
FGLY391
FHOH608

site_idAE4
Number of Residues12
Detailsbinding site for residue H9V F 502
ChainResidue
EASP64
EGLY66
EASP136
FVAL30
FLEU34
FILE184
FASN185
FPHE188
FPHE202
FPRO208
FPHE211
FHIS294

site_idAE5
Number of Residues5
Detailsbinding site for residue CS F 503
ChainResidue
FGLY246
FALA282
FTHR284
FTYR320
FGLY322

site_idAE6
Number of Residues6
Detailsbinding site for residue MLA F 506
ChainResidue
DASP143
FCYS137
FGLY141
FLEU142
FGLY167
HHOH601

site_idAE7
Number of Residues3
Detailsbinding site for residue PGE F 507
ChainResidue
FPRO262
FARG265
FGLY334

site_idAE8
Number of Residues6
Detailsbinding site for residue MLA G 501
ChainResidue
GTYR181
GGLY217
GLEU218
GGLY219
GGLY239
GSER240

site_idAE9
Number of Residues2
Detailsbinding site for residue FMT H 501
ChainResidue
FLEU165
HARG355

site_idAF1
Number of Residues18
Detailsbinding site for residue P1T H 502
ChainResidue
HHIS100
HLYS101
HTHR124
HGLY125
HALA126
HGLY127
HGLN128
HHIS129
HTHR204
HGLY246
HGLY247
HGLY248
HSER249
HASN250
HGLY317
HGLU364
HSER390
HHOH611

site_idAF2
Number of Residues12
Detailsbinding site for residue H9V H 503
ChainResidue
GASP64
GGLY66
GASP136
HVAL30
HLEU34
HILE184
HASN185
HPHE188
HPHE202
HPRO208
HPHE211
HHIS294

site_idAF3
Number of Residues5
Detailsbinding site for residue CS H 504
ChainResidue
HGLY246
HALA282
HTHR284
HTYR320
HGLY322

site_idAF4
Number of Residues3
Detailsbinding site for residue FMT H 505
ChainResidue
GGLN144
HSER23
HPHE297

site_idAF5
Number of Residues2
Detailsbinding site for residue EDO H 506
ChainResidue
HARG265
HFMT507

site_idAF6
Number of Residues5
Detailsbinding site for residue FMT H 507
ChainResidue
HARG265
HLEU266
HARG335
HASP337
HEDO506

site_idAF7
Number of Residues2
Detailsbinding site for residue FMT H 508
ChainResidue
HARG119
HASN194

Functional Information from PROSITE/UniProt
site_idPS00167
Number of Residues14
DetailsTRP_SYNTHASE_ALPHA Tryptophan synthase alpha chain signature. IEVGvPYSDPGMDG
ChainResidueDetails
AILE56-GLY69

site_idPS00168
Number of Residues15
DetailsTRP_SYNTHASE_BETA Tryptophan synthase beta chain pyridoxal-phosphate attachment site. LnHtGSHKiNnvLgQ
ChainResidueDetails
BLEU94-GLN108

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsMOD_RES: N6-(pyridoxal phosphate)lysine => ECO:0000255|HAMAP-Rule:MF_00133
ChainResidueDetails
BHIS100
DHIS100
FHIS100
HHIS100
EGLU57
EASP68
GGLU57
GASP68

227111

PDB entries from 2024-11-06

PDB statisticsPDBj update infoContact PDBjnumon