Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

5TCJ

Crystal structure of tryptophan synthase from M. tuberculosis - aminoacrylate and BRD4592-bound form

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000162	biological_process	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	tryptophan metabolic process
A	0016829	molecular_function	lyase activity
B	0000162	biological_process	tryptophan biosynthetic process
B	0004834	molecular_function	tryptophan synthase activity
B	0005737	cellular_component	cytoplasm
B	0006568	biological_process	tryptophan metabolic process
B	0016829	molecular_function	lyase activity
B	1901605	biological_process	alpha-amino acid metabolic process
C	0000162	biological_process	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	tryptophan metabolic process
C	0016829	molecular_function	lyase activity
D	0000162	biological_process	tryptophan biosynthetic process
D	0004834	molecular_function	tryptophan synthase activity
D	0005737	cellular_component	cytoplasm
D	0006568	biological_process	tryptophan metabolic process
D	0016829	molecular_function	lyase activity
D	1901605	biological_process	alpha-amino acid metabolic process
E	0000162	biological_process	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	tryptophan metabolic process
E	0016829	molecular_function	lyase activity
F	0000162	biological_process	tryptophan biosynthetic process
F	0004834	molecular_function	tryptophan synthase activity
F	0005737	cellular_component	cytoplasm
F	0006568	biological_process	tryptophan metabolic process
F	0016829	molecular_function	lyase activity
F	1901605	biological_process	alpha-amino acid metabolic process
G	0000162	biological_process	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	tryptophan metabolic process
G	0016829	molecular_function	lyase activity
H	0000162	biological_process	tryptophan biosynthetic process
H	0004834	molecular_function	tryptophan synthase activity
H	0005737	cellular_component	cytoplasm
H	0006568	biological_process	tryptophan metabolic 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	9
Details	binding site for residue MLI A 301

Chain	Residue
A	TYR181
A	GLY217
A	LEU218
A	GLY219
A	VAL220
A	ILE237
A	GLY239
A	SER240
A	FMT302

site_id	AC2
Number of Residues	5
Details	binding site for residue FMT A 302

Chain	Residue
A	TYR30
A	GLU57
A	TYR181
A	ILE237
A	MLI301

site_id	AC3
Number of Residues	21
Details	binding site for residue P1T B 501

Chain	Residue
B	HIS100
B	LYS101
B	THR124
B	GLY125
B	ALA126
B	GLY127
B	GLN128
B	HIS129
B	LEU180
B	THR204
B	CYS244
B	GLY246
B	GLY247
B	GLY248
B	SER249
B	ASN250
B	GLY317
B	GLU364
B	SER390
B	GLY391
B	HOH626

site_id	AC4
Number of Residues	6
Details	binding site for residue CS B 502

Chain	Residue
B	GLY246
B	ALA282
B	THR284
B	TYR320
B	GLY322
B	HOH613

site_id	AC5
Number of Residues	6
Details	binding site for residue CS B 503

Chain	Residue
B	GLY67
B	PRO69
B	HOH738
B	HOH739
D	GLY67
D	PRO69

site_id	AC6
Number of Residues	4
Details	binding site for residue CS B 504

Chain	Residue
B	LYS402
B	TRP403
H	LYS402
H	TRP403

site_id	AC7
Number of Residues	12
Details	binding site for residue 79V B 505

Chain	Residue
A	ASP64
A	GLY66
A	MET67
A	ASP136
B	PRO31
B	LEU34
B	PHE188
B	PHE202
B	PRO208
B	HIS294
B	GLY295
B	HOH661

site_id	AC8
Number of Residues	3
Details	binding site for residue FMT B 506

Chain	Residue
B	LYS47
B	GLU48
B	HOH658

site_id	AC9
Number of Residues	2
Details	binding site for residue FMT B 507

Chain	Residue
B	ARG355
D	LEU165

site_id	AD1
Number of Residues	3
Details	binding site for residue FMT B 508

Chain	Residue
B	GLN80
B	HOH709
F	ARG119

site_id	AD2
Number of Residues	2
Details	binding site for residue FMT B 509

Chain	Residue
B	LEU165
D	ARG355

site_id	AD3
Number of Residues	8
Details	binding site for residue MLI G 301

Chain	Residue
G	TYR181
G	GLY217
G	LEU218
G	GLY219
G	GLY239
G	SER240
G	FMT303
G	HOH431

site_id	AD4
Number of Residues	5
Details	binding site for residue FMT G 302

Chain	Residue
A	HOH418
G	ARG223
G	GLY258
G	ALA262
G	HOH447

site_id	AD5
Number of Residues	4
Details	binding site for residue FMT G 303

Chain	Residue
G	GLU57
G	TYR181
G	ILE237
G	MLI301

site_id	AD6
Number of Residues	3
Details	binding site for residue FMT G 304

Chain	Residue
G	ASN22
G	ARG24
G	ARG265

site_id	AD7
Number of Residues	22
Details	binding site for residue P1T H 501

Chain	Residue
H	GLN128
H	HIS129
H	LEU180
H	THR204
H	CYS244
H	GLY246
H	GLY247
H	GLY248
H	SER249
H	ASN250
H	GLY317
H	GLU364
H	SER390
H	GLY391
H	HOH649
H	HOH698
H	HIS100
H	LYS101
H	THR124
H	GLY125
H	ALA126
H	GLY127

site_id	AD8
Number of Residues	5
Details	binding site for residue CS H 502

Chain	Residue
H	GLY246
H	ALA282
H	THR284
H	TYR320
H	GLY322

site_id	AD9
Number of Residues	10
Details	binding site for residue 79V H 503

Chain	Residue
G	ASP64
G	MET67
G	TYR108
G	ASP136
H	LEU34
H	PHE188
H	PHE202
H	PRO208
H	HIS294
H	GLY295

site_id	AE1
Number of Residues	6
Details	binding site for residue FMT H 504

Chain	Residue
D	ARG119
D	VAL145
D	HOH704
H	ARG77
H	GLN80
H	HOH700

site_id	AE2
Number of Residues	2
Details	binding site for residue FMT H 505

Chain	Residue
H	GLU48
H	ARG114

site_id	AE3
Number of Residues	2
Details	binding site for residue FMT H 506

Chain	Residue
H	HOH620
H	HOH646

site_id	AE4
Number of Residues	2
Details	binding site for residue FMT H 507

Chain	Residue
F	ARG355
H	LEU165

site_id	AE5
Number of Residues	2
Details	binding site for residue FMT H 508

Chain	Residue
D	ASN194
H	SER84

site_id	AE6
Number of Residues	6
Details	binding site for residue MLI E 301

Chain	Residue
E	TYR181
E	GLY217
E	LEU218
E	GLY219
E	GLY239
E	SER240

site_id	AE7
Number of Residues	20
Details	binding site for residue P1T F 501

Chain	Residue
F	HIS100
F	LYS101
F	THR124
F	GLY125
F	ALA126
F	GLY127
F	GLN128
F	HIS129
F	THR204
F	CYS244
F	GLY246
F	GLY247
F	GLY248
F	SER249
F	ASN250
F	GLY317
F	GLU364
F	SER390
F	GLY391
F	HOH644

site_id	AE8
Number of Residues	6
Details	binding site for residue CS F 502

Chain	Residue
F	GLY246
F	ALA282
F	THR284
F	TYR320
F	GLY322
F	HOH616

site_id	AE9
Number of Residues	2
Details	binding site for residue CS F 503

Chain	Residue
D	HOH721
F	LEU142

site_id	AF1
Number of Residues	6
Details	binding site for residue CS F 504

Chain	Residue
F	GLY67
F	PRO69
F	HOH715
H	GLY67
H	PRO69
H	HOH736

site_id	AF2
Number of Residues	10
Details	binding site for residue 79V F 505

Chain	Residue
E	ASP64
E	GLY66
E	ASP136
F	PRO31
F	LEU34
F	PHE188
F	TYR200
F	PHE202
F	PRO208
F	HIS294

site_id	AF3
Number of Residues	7
Details	binding site for residue FMT F 506

Chain	Residue
D	GLY141
D	LEU142
D	ASP143
D	CS503
F	GLY141
F	LEU142
F	ASP143

site_id	AF4
Number of Residues	3
Details	binding site for residue FMT F 507

Chain	Residue
F	LYS47
F	GLU48
F	ARG114

site_id	AF5
Number of Residues	2
Details	binding site for residue FMT F 508

Chain	Residue
E	GLN144
F	SER23

site_id	AF6
Number of Residues	3
Details	binding site for residue FMT F 509

Chain	Residue
F	LEU165
H	ARG355
H	PHE404

site_id	AF7
Number of Residues	5
Details	binding site for residue FMT F 510

Chain	Residue
F	ASP274
F	ARG280
F	HIS312
F	SER313
F	ASP343

site_id	AF8
Number of Residues	6
Details	binding site for residue MLI C 301

Chain	Residue
C	TYR181
C	GLY217
C	GLY219
C	ILE237
C	GLY239
C	SER240

site_id	AF9
Number of Residues	2
Details	binding site for residue FMT C 302

Chain	Residue
C	GLN144
D	SER23

site_id	AG1
Number of Residues	22
Details	binding site for residue P1T D 501

Chain	Residue
D	HIS100
D	LYS101
D	THR124
D	GLY125
D	ALA126
D	GLY127
D	GLN128
D	HIS129
D	THR204
D	CYS244
D	GLY246
D	GLY247
D	GLY248
D	SER249
D	ASN250
D	GLY317
D	LEU318
D	GLU364
D	SER390
D	GLY391
D	HOH644
D	HOH658

site_id	AG2
Number of Residues	7
Details	binding site for residue CS D 502

Chain	Residue
D	GLY246
D	ALA282
D	THR284
D	TYR320
D	GLY322
D	HOH648
D	HOH685

site_id	AG3
Number of Residues	3
Details	binding site for residue CS D 503

Chain	Residue
D	LEU142
F	FMT506
F	HOH700

site_id	AG4
Number of Residues	9
Details	binding site for residue 79V D 504

Chain	Residue
C	ASP64
C	GLY66
C	MET67
D	LEU34
D	PHE188
D	PHE202
D	PRO208
D	HIS294
D	GLY295

site_id	AG5
Number of Residues	2
Details	binding site for residue FMT D 505

Chain	Residue
D	LYS47
D	GLU48

site_id	AG6
Number of Residues	3
Details	binding site for residue FMT D 506

Chain	Residue
D	HIS312
D	SER313
D	ASP319

site_id	AG7
Number of Residues	2
Details	binding site for residue FMT D 507

Chain	Residue
D	ALA36
D	GLU40

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	4
Details	MOD_RES: N6-(pyridoxal phosphate)lysine => ECO:0000255\|HAMAP-Rule:MF_00133

Chain	Residue	Details
B	HIS100
H	HIS100
F	HIS100
D	HIS100
E	GLU57
E	ASP68
C	GLU57
C	ASP68

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