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

6VFD

Tryptophan synthase mutant Q114A in complex with cesium ion at the metal coordination site and 2-aminophenol quinonoid at the enzyme beta site

Functional Information from GO Data
ChainGOidnamespacecontents
A0000162biological_processtryptophan biosynthetic process
A0004834molecular_functiontryptophan synthase activity
A0005515molecular_functionprotein binding
A0005829cellular_componentcytosol
A0006568biological_processtryptophan metabolic process
A0016829molecular_functionlyase activity
B0000162biological_processtryptophan biosynthetic process
B0004834molecular_functiontryptophan synthase activity
B0005515molecular_functionprotein binding
B0005737cellular_componentcytoplasm
B0006568biological_processtryptophan metabolic process
B0016829molecular_functionlyase activity
B0042802molecular_functionidentical protein binding
Functional Information from PDB Data
site_idAC1
Number of Residues7
Detailsbinding site for residue EDO A 301
ChainResidue
APHE107
AASN108
AHOH421
AHOH483
AHOH536
BARG275
BVAL276

site_idAC2
Number of Residues6
Detailsbinding site for residue EDO A 302
ChainResidue
AILE64
ATYR175
AGLY234
AHOH546
APHE22
AGLU49

site_idAC3
Number of Residues6
Detailsbinding site for residue SER A 303
ChainResidue
APHE82
APHE114
AARG117
AHOH406
AHOH454
AHOH455

site_idAC4
Number of Residues5
Detailsbinding site for residue DMS A 304
ChainResidue
AILE41
AHIS92
APRO93
ATHR94
AILE95

site_idAC5
Number of Residues3
Detailsbinding site for residue CL A 305
ChainResidue
AALA167
AGLY170
AHIS204

site_idAC6
Number of Residues1
Detailsbinding site for residue CL A 306
ChainResidue
AHOH546

site_idAC7
Number of Residues21
Detailsbinding site for residue 1D0 B 401
ChainResidue
BALA85
BHIS86
BLYS87
BGLU109
BTHR110
BGLY111
BGLY113
BALA114
BHIS115
BTHR190
BCYS230
BGLY232
BGLY233
BGLY234
BSER235
BASN236
BGLY303
BGLU350
BSER377
BHOH601
BHOH604

site_idAC8
Number of Residues5
Detailsbinding site for residue SER B 402
ChainResidue
BTYR8
BPHE9
BGLY10
BTYR315
BHOH621

site_idAC9
Number of Residues3
Detailsbinding site for residue EDO B 403
ChainResidue
BTHR289
BALA290
BASP291

site_idAD1
Number of Residues3
Detailsbinding site for residue EDO B 404
ChainResidue
BLYS219
BGLU220
BCL430

site_idAD2
Number of Residues2
Detailsbinding site for residue DMS B 405
ChainResidue
BILE262
BHIS267

site_idAD3
Number of Residues2
Detailsbinding site for residue DMS B 406
ChainResidue
BGLU331
BHOH780

site_idAD4
Number of Residues5
Detailsbinding site for residue DMS B 407
ChainResidue
BSER143
BPRO144
BPHE147
BPHE385
BHIS388

site_idAD5
Number of Residues3
Detailsbinding site for residue DMS B 408
ChainResidue
BTYR8
BGLY10
BHOH774

site_idAD6
Number of Residues8
Detailsbinding site for residue DMS B 409
ChainResidue
BLYS50
BGLY54
BARG55
BPRO56
BTHR57
BGLN215
BCS416
BCS416

site_idAD7
Number of Residues4
Detailsbinding site for residue DMS B 410
ChainResidue
BLEU271
BARG363
BGLU364
BHOH815

site_idAD8
Number of Residues4
Detailsbinding site for residue DMS B 411
ChainResidue
BGLN42
BALA46
BMET207
BHOH854

site_idAD9
Number of Residues3
Detailsbinding site for residue DMS B 412
ChainResidue
BTHR3
BLEU4
BLEU5

site_idAE1
Number of Residues4
Detailsbinding site for residue DMS B 413
ChainResidue
BGLU211
BHOH681
BHOH846
BHOH894

site_idAE2
Number of Residues3
Detailsbinding site for residue CS B 414
ChainResidue
BTHR66
BTHR69
BTHR71

site_idAE3
Number of Residues7
Detailsbinding site for residue CS B 415
ChainResidue
BGLY232
BGLU256
BGLY268
BLEU304
BPHE306
BSER308
BVAL231

site_idAE4
Number of Residues6
Detailsbinding site for residue CS B 416
ChainResidue
BGLY54
BGLY54
BPRO56
BPRO56
BDMS409
BDMS409

site_idAE5
Number of Residues1
Detailsbinding site for residue CL B 417
ChainResidue
BGLN36

site_idAE6
Number of Residues2
Detailsbinding site for residue CL B 419
ChainResidue
BASP225
BSER249

site_idAE7
Number of Residues1
Detailsbinding site for residue CL B 420
ChainResidue
BHOH776

site_idAE8
Number of Residues3
Detailsbinding site for residue CL B 421
ChainResidue
BHOH533
BHOH720
BHOH958

site_idAE9
Number of Residues2
Detailsbinding site for residue CL B 422
ChainResidue
BARG321
BHOH952

site_idAF1
Number of Residues1
Detailsbinding site for residue CL B 424
ChainResidue
BGLU155

site_idAF2
Number of Residues2
Detailsbinding site for residue CL B 426
ChainResidue
BGLN36
BLYS37

site_idAF3
Number of Residues4
Detailsbinding site for residue CL B 427
ChainResidue
BGLU369
BHOH515
BHOH672
BHOH779

site_idAF4
Number of Residues2
Detailsbinding site for residue CL B 428
ChainResidue
BTHR248
BHOH904

site_idAF5
Number of Residues1
Detailsbinding site for residue CL B 429
ChainResidue
BHOH516

site_idAF6
Number of Residues2
Detailsbinding site for residue CL B 430
ChainResidue
BLYS219
BEDO404

Functional Information from PROSITE/UniProt
site_idPS00167
Number of Residues14
DetailsTRP_SYNTHASE_ALPHA Tryptophan synthase alpha chain signature. LELGvPFSDPLADG
ChainResidueDetails
ALEU48-GLY61

site_idPS00168
Number of Residues15
DetailsTRP_SYNTHASE_BETA Tryptophan synthase beta chain pyridoxal-phosphate attachment site. LlHgGAHKtNqvLgQ
ChainResidueDetails
BLEU80-GLN94

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsMOD_RES: N6-(pyridoxal phosphate)lysine
ChainResidueDetails
BLYS87
AASP60

Catalytic Information from CSA
site_idMCSA1
Number of Residues3
DetailsM-CSA 383
ChainResidueDetails
BLYS87electron pair acceptor, electron pair donor, nucleofuge, nucleophile, proton acceptor, proton donor
BGLU109
BSER377hydrogen bond donor

221051

PDB entries from 2024-06-12

PDB statisticsPDBj update infoContact PDBjnumon