Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

5TCI

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

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	7
Details	binding site for residue MLI A 301

Chain	Residue
A	TYR181
A	GLY217
A	LEU218
A	GLY219
A	GLY239
A	SER240
A	HOH410

site_id	AC2
Number of Residues	4
Details	binding site for residue FMT A 302

Chain	Residue
A	TYR181
A	ILE237
A	GLU57
A	MET106

site_id	AC3
Number of Residues	13
Details	binding site for residue 79V B 501

Chain	Residue
A	ASP64
A	GLY66
A	TYR108
A	ASP136
A	HOH409
B	PRO31
B	TRP191
B	TYR200
B	PHE202
B	PRO208
B	PHE211
B	HIS294
B	GLY295

site_id	AC4
Number of Residues	2
Details	binding site for residue FMT B 502

Chain	Residue
B	LYS47
B	GLU48

site_id	AC5
Number of Residues	4
Details	binding site for residue FMT B 503

Chain	Residue
B	ARG265
B	ASP337
B	ARG339
B	GLU378

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

Chain	Residue
B	LYS402
B	GLY405
B	HOH682
H	TRP403

site_id	AC7
Number of Residues	7
Details	binding site for residue MLI G 301

Chain	Residue
G	TYR181
G	GLY217
G	LEU218
G	GLY219
G	GLY239
G	SER240
G	HOH416

site_id	AC8
Number of Residues	3
Details	binding site for residue FMT G 302

Chain	Residue
G	GLU57
G	MET106
G	TYR181

site_id	AC9
Number of Residues	2
Details	binding site for residue FMT G 303

Chain	Residue
G	GLN144
H	SER23

site_id	AD1
Number of Residues	16
Details	binding site for residue 79V H 501

Chain	Residue
G	ASP64
G	GLY66
G	TYR108
G	ASP136
H	VAL30
H	PRO31
H	LEU34
H	PHE188
H	TRP191
H	TYR200
H	PHE202
H	GLY207
H	PRO208
H	PHE211
H	HIS294
H	GLY295

site_id	AD2
Number of Residues	4
Details	binding site for residue FMT H 502

Chain	Residue
H	ARG265
H	ASP337
H	GLU378
H	HOH627

site_id	AD3
Number of Residues	4
Details	binding site for residue FMT H 503

Chain	Residue
H	LYS47
H	GLU48
H	ARG114
H	HOH637

site_id	AD4
Number of Residues	5
Details	binding site for residue MLI E 301

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

site_id	AD5
Number of Residues	9
Details	binding site for residue 79V F 501

Chain	Residue
E	ASP64
E	GLY66
E	MET67
F	PRO31
F	LEU34
F	PHE188
F	PHE202
F	PRO208
F	HIS294

site_id	AD6
Number of Residues	2
Details	binding site for residue FMT F 503

Chain	Residue
F	GLU48
F	ARG114

site_id	AD7
Number of Residues	6
Details	binding site for residue MLI C 301

Chain	Residue
C	TYR181
C	THR185
C	GLY217
C	GLY219
C	GLY239
C	SER240

site_id	AD8
Number of Residues	3
Details	binding site for residue FMT C 302

Chain	Residue
C	GLU57
C	TYR181
C	ILE237

site_id	AD9
Number of Residues	11
Details	binding site for residue 79V D 501

Chain	Residue
D	PRO31
D	LEU34
D	ASN185
D	PHE188
D	PHE202
D	PRO208
D	HIS294
C	ASP64
C	GLY66
C	MET67
C	ASP136

site_id	AE1
Number of Residues	3
Details	binding site for residue FMT D 502

Chain	Residue
D	LYS47
D	GLU48
D	ARG114

site_id	AE2
Number of Residues	1
Details	binding site for residue FMT D 503

Chain	Residue
D	LEU259

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)