Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

6E9P

Crystal structure of tryptophan synthase from M. tuberculosis - open form with BRD0059 bound

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000162	biological_process	L-tryptophan biosynthetic process
A	0004834	molecular_function	tryptophan synthase activity
A	0005829	cellular_component	cytosol
A	0005886	cellular_component	plasma membrane
A	0006568	biological_process	L-tryptophan metabolic process
A	0008652	biological_process	amino acid biosynthetic process
A	0009073	biological_process	aromatic amino acid family biosynthetic process
A	0016829	molecular_function	lyase activity
B	0000162	biological_process	L-tryptophan biosynthetic process
B	0004834	molecular_function	tryptophan synthase activity
B	0005737	cellular_component	cytoplasm
B	0006568	biological_process	L-tryptophan metabolic process
B	0008652	biological_process	amino acid biosynthetic process
B	0009073	biological_process	aromatic amino acid family biosynthetic process
B	0016829	molecular_function	lyase activity
B	1901605	biological_process	alpha-amino acid metabolic process
C	0000162	biological_process	L-tryptophan biosynthetic process
C	0004834	molecular_function	tryptophan synthase activity
C	0005829	cellular_component	cytosol
C	0005886	cellular_component	plasma membrane
C	0006568	biological_process	L-tryptophan metabolic process
C	0008652	biological_process	amino acid biosynthetic process
C	0009073	biological_process	aromatic amino acid family biosynthetic process
C	0016829	molecular_function	lyase activity
D	0000162	biological_process	L-tryptophan biosynthetic process
D	0004834	molecular_function	tryptophan synthase activity
D	0005737	cellular_component	cytoplasm
D	0006568	biological_process	L-tryptophan metabolic process
D	0008652	biological_process	amino acid biosynthetic process
D	0009073	biological_process	aromatic amino acid family biosynthetic process
D	0016829	molecular_function	lyase activity
D	1901605	biological_process	alpha-amino acid metabolic process
E	0000162	biological_process	L-tryptophan biosynthetic process
E	0004834	molecular_function	tryptophan synthase activity
E	0005829	cellular_component	cytosol
E	0005886	cellular_component	plasma membrane
E	0006568	biological_process	L-tryptophan metabolic process
E	0008652	biological_process	amino acid biosynthetic process
E	0009073	biological_process	aromatic amino acid family biosynthetic process
E	0016829	molecular_function	lyase activity
F	0000162	biological_process	L-tryptophan biosynthetic process
F	0004834	molecular_function	tryptophan synthase activity
F	0005737	cellular_component	cytoplasm
F	0006568	biological_process	L-tryptophan metabolic process
F	0008652	biological_process	amino acid biosynthetic process
F	0009073	biological_process	aromatic amino acid family biosynthetic process
F	0016829	molecular_function	lyase activity
F	1901605	biological_process	alpha-amino acid metabolic process
G	0000162	biological_process	L-tryptophan biosynthetic process
G	0004834	molecular_function	tryptophan synthase activity
G	0005829	cellular_component	cytosol
G	0005886	cellular_component	plasma membrane
G	0006568	biological_process	L-tryptophan metabolic process
G	0008652	biological_process	amino acid biosynthetic process
G	0009073	biological_process	aromatic amino acid family biosynthetic process
G	0016829	molecular_function	lyase activity
H	0000162	biological_process	L-tryptophan biosynthetic process
H	0004834	molecular_function	tryptophan synthase activity
H	0005737	cellular_component	cytoplasm
H	0006568	biological_process	L-tryptophan metabolic process
H	0008652	biological_process	amino acid biosynthetic process
H	0009073	biological_process	aromatic amino acid family biosynthetic process
H	0016829	molecular_function	lyase activity
H	1901605	biological_process	alpha-amino acid metabolic process

Functional Information from PDB Data

site_id	AC1
Number of Residues	8
Details	binding site for residue MLA A 501

Chain	Residue
A	TYR181
A	GLY217
A	LEU218
A	GLY219
A	GLY239
A	SER240
A	HOH602
A	HOH609

site_id	AC2
Number of Residues	5
Details	binding site for residue ACT A 502

Chain	Residue
A	PRO70
A	THR71
A	SER240
A	HOH605
A	GLY69

site_id	AC3
Number of Residues	9
Details	binding site for residue EDO A 503

Chain	Residue
A	TYR30
A	VAL60
A	PRO61
A	TYR62
A	PRO65
A	ASP68
A	THR76
A	MET106
A	TYR108

site_id	AC4
Number of Residues	13
Details	binding site for residue HDJ B 501

Chain	Residue
A	ASP64
A	GLY66
A	MET67
A	TYR108
B	LEU34
B	ILE184
B	ASN185
B	PHE188
B	PHE202
B	PRO208
B	PHE211
B	HIS294
B	GLY295

site_id	AC5
Number of Residues	10
Details	binding site for residue MLT B 502

Chain	Residue
B	ASP57
B	ARG60
B	LEU61
B	LEU110
B	ARG113
B	LEU140
B	HOH601
B	HOH633
F	GLN231
F	GLY232

site_id	AC6
Number of Residues	3
Details	binding site for residue FMT B 503

Chain	Residue
B	GLY351
B	ARG355
H	LEU165

site_id	AC7
Number of Residues	5
Details	binding site for residue ACT B 504

Chain	Residue
B	HIS11
B	ASP12
B	GLY20
B	TRP329
G	GLN231

site_id	AC8
Number of Residues	7
Details	binding site for residue FMT B 505

Chain	Residue
B	GLU74
B	ALA75
B	THR76
B	SER79
B	ALA85
B	ARG86
B	ILE87

site_id	AC9
Number of Residues	3
Details	binding site for residue ACT B 506

Chain	Residue
B	LEU237
B	PRO238
B	GLY263

site_id	AD1
Number of Residues	3
Details	binding site for residue FMT B 507

Chain	Residue
A	GLN144
B	SER23
B	PHE297

site_id	AD2
Number of Residues	6
Details	binding site for residue FMT B 508

Chain	Residue
B	VAL245
B	GLY246
B	ALA282
B	THR284
B	TYR320
B	GLY322

site_id	AD3
Number of Residues	2
Details	binding site for residue FMT B 509

Chain	Residue
B	GLU48
B	ARG114

site_id	AD4
Number of Residues	3
Details	binding site for residue FMT B 510

Chain	Residue
B	HIS11
B	GLU326
B	TRP329

site_id	AD5
Number of Residues	3
Details	binding site for residue EDO B 511

Chain	Residue
B	PRO262
B	GLY263
B	ARG265

site_id	AD6
Number of Residues	8
Details	binding site for residue MLA C 501

Chain	Residue
C	TYR181
C	GLY217
C	LEU218
C	GLY219
C	GLY239
C	SER240
C	HOH604
C	HOH607

site_id	AD7
Number of Residues	4
Details	binding site for residue FMT C 502

Chain	Residue
C	GLY116
C	VAL117
C	ASP118
C	ALA119

site_id	AD8
Number of Residues	3
Details	binding site for residue FMT C 503

Chain	Residue
C	PRO39
C	VAL42
C	ALA43

site_id	AD9
Number of Residues	3
Details	binding site for residue FMT C 504

Chain	Residue
C	LEU113
C	GLN144
D	SER23

site_id	AE1
Number of Residues	11
Details	binding site for residue HDJ D 501

Chain	Residue
C	MET67
D	LEU34
D	ILE184
D	ASN185
D	PHE188
D	PHE202
D	PRO208
D	PHE211
D	HIS294
D	GLY295
C	ASP64

site_id	AE2
Number of Residues	1
Details	binding site for residue FMT D 502

Chain	Residue
D	ARG335

site_id	AE3
Number of Residues	3
Details	binding site for residue FMT D 503

Chain	Residue
B	LYS402
B	GLY405
D	TRP403

site_id	AE4
Number of Residues	3
Details	binding site for residue FMT D 504

Chain	Residue
D	HIS11
D	ASP12
D	GLY20

site_id	AE5
Number of Residues	2
Details	binding site for residue FMT D 505

Chain	Residue
B	ARG60
D	ASN64

site_id	AE6
Number of Residues	1
Details	binding site for residue FMT D 506

Chain	Residue
H	ASN194

site_id	AE7
Number of Residues	5
Details	binding site for residue FMT D 507

Chain	Residue
D	ARG265
D	LEU266
D	ARG335
D	ASP337
D	EDO510

site_id	AE8
Number of Residues	3
Details	binding site for residue EDO D 508

Chain	Residue
B	TRP403
B	HOH611
D	LYS402

site_id	AE9
Number of Residues	6
Details	binding site for residue EDO D 509

Chain	Residue
D	THR124
D	GLY125
D	ALA126
D	GLY127
D	GLN128
D	HIS129

site_id	AF1
Number of Residues	4
Details	binding site for residue EDO D 510

Chain	Residue
D	PRO262
D	GLY263
D	ARG265
D	FMT507

site_id	AF2
Number of Residues	4
Details	binding site for residue EDO D 511

Chain	Residue
B	GLY273
B	THR342
B	SER344
D	ASN409

site_id	AF3
Number of Residues	7
Details	binding site for residue FMT D 512

Chain	Residue
D	GLY291
D	PHE293
D	SER296
D	SER298
D	TYR299
D	GLY322
D	VAL323

site_id	AF4
Number of Residues	4
Details	binding site for residue FMT D 513

Chain	Residue
D	ALA44
D	LYS47
D	GLU48
D	ARG114

site_id	AF5
Number of Residues	3
Details	binding site for residue FMT D 514

Chain	Residue
D	SER23
D	GLY24
D	GLU332

site_id	AF6
Number of Residues	5
Details	binding site for residue FMT D 515

Chain	Residue
D	TYR73
D	THR76
D	ARG77
D	GLU357
F	LEU139

site_id	AF7
Number of Residues	7
Details	binding site for residue FMT D 516

Chain	Residue
D	VAL245
D	GLY246
D	GLU270
D	ALA282
D	THR284
D	TYR320
D	GLY322

site_id	AF8
Number of Residues	4
Details	binding site for residue EDO E 501

Chain	Residue
E	TYR181
E	GLY217
E	GLY239
E	SER240

site_id	AF9
Number of Residues	12
Details	binding site for residue HDJ F 501

Chain	Residue
E	ASP64
E	GLY66
E	MET67
F	LEU34
F	ILE184
F	ASN185
F	PHE188
F	PHE202
F	PRO208
F	PHE211
F	HIS294
F	GLY295

site_id	AG1
Number of Residues	1
Details	binding site for residue FMT F 502

Chain	Residue
F	SER23

site_id	AG2
Number of Residues	2
Details	binding site for residue FMT F 504

Chain	Residue
F	VAL160
F	VAL170

site_id	AG3
Number of Residues	4
Details	binding site for residue FMT F 505

Chain	Residue
F	GLU345
F	ALA349
F	ALA370
F	LEU373

site_id	AG4
Number of Residues	2
Details	binding site for residue EDO F 506

Chain	Residue
F	PRO262
F	ARG265

site_id	AG5
Number of Residues	5
Details	binding site for residue EDO F 507

Chain	Residue
D	LEU139
F	TYR73
F	THR76
F	ARG77
F	GLU357

site_id	AG6
Number of Residues	5
Details	binding site for residue EDO F 508

Chain	Residue
F	ARG236
H	SER79
H	GLN80
H	SER84
H	ARG381

site_id	AG7
Number of Residues	4
Details	binding site for residue ACT G 501

Chain	Residue
G	MET67
G	ASP68
G	MET106
G	TYR181

site_id	AG8
Number of Residues	5
Details	binding site for residue EDO G 502

Chain	Residue
G	TYR181
G	THR185
G	GLY217
G	GLY239
G	SER240

site_id	AG9
Number of Residues	2
Details	binding site for residue ACT G 503

Chain	Residue
G	GLN144
H	SER23

site_id	AH1
Number of Residues	14
Details	binding site for residue HDJ H 501

Chain	Residue
G	ASP64
G	GLY66
G	MET67
G	TYR108
G	ASP136
H	LEU34
H	ILE184
H	ASN185
H	PHE188
H	PHE202
H	PRO208
H	PHE211
H	HIS294
H	GLY295

site_id	AH2
Number of Residues	3
Details	binding site for residue FMT H 502

Chain	Residue
H	PRO238
H	ASP239
H	GLY263

site_id	AH3
Number of Residues	1
Details	binding site for residue FMT H 503

Chain	Residue
H	ASP217

site_id	AH4
Number of Residues	3
Details	binding site for residue FMT H 504

Chain	Residue
H	LYS47
H	GLU48
H	ARG114

site_id	AH5
Number of Residues	6
Details	binding site for residue FMT H 505

Chain	Residue
B	PRO69
B	PRO71
D	GLN52
H	ALA63
H	GLY67
H	ARG68

site_id	AH6
Number of Residues	4
Details	binding site for residue EDO H 506

Chain	Residue
H	GLN128
H	ASN159
H	ARG162
H	LYS395

site_id	AH7
Number of Residues	3
Details	binding site for residue EDO H 507

Chain	Residue
H	PRO262
H	GLY263
H	ARG265

site_id	AH8
Number of Residues	3
Details	binding site for residue FMT H 508

Chain	Residue
H	ALA36
H	GLU40
H	ALA195

Functional Information from PROSITE/UniProt

site_id	PS00167
Number of Residues	14
Details	TRP_SYNTHASE_ALPHA Tryptophan synthase alpha chain signature. IEVGvPYSDPGMDG

Chain	Residue	Details
A	ILE56-GLY69

site_id	PS00168
Number of Residues	15
Details	TRP_SYNTHASE_BETA Tryptophan synthase beta chain pyridoxal-phosphate attachment site. LnHtGSHKiNnvLgQ

Chain	Residue	Details
B	LEU94-GLN108

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	8
Details	Active site: {"description":"Proton acceptor","evidences":[{"source":"HAMAP-Rule","id":"MF_00131","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	4
Details	Modified residue: {"description":"N6-(pyridoxal phosphate)lysine","evidences":[{"source":"HAMAP-Rule","id":"MF_00133","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

		Sequence (fasta)
		PDBx/mmCIF
		PDBML format (no-atom)
		PDB format (full)
		Validation report (PDF)
		EDMap 2fo-fc (MTZ)