Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

5TCH

Crystal structure of tryptophan synthase from M. tuberculosis - ligand-free form, TrpA-G66V mutant

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	GLY239
A	SER240
A	FMT302
A	HOH405
A	HOH416

site_id	AC2
Number of Residues	6
Details	binding site for residue FMT A 302

Chain	Residue
A	TYR30
A	GLU57
A	MET106
A	TYR181
A	ILE237
A	MLI301

site_id	AC3
Number of Residues	7
Details	binding site for residue MLI B 501

Chain	Residue
B	THR124
B	GLY125
B	ALA126
B	GLN128
B	HIS129
B	LEU180
B	ALA316

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	3
Details	binding site for residue FMT B 503

Chain	Residue
B	ARG265
B	ASP337
B	GLU378

site_id	AC6
Number of Residues	3
Details	binding site for residue FMT B 504

Chain	Residue
A	GLN144
B	SER23
B	TYR29

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

Chain	Residue
G	TYR181
G	GLY217
G	GLY219
G	GLY239
G	SER240
G	FMT302
G	HOH406

site_id	AC8
Number of Residues	5
Details	binding site for residue FMT G 302

Chain	Residue
G	TYR30
G	GLU57
G	MET106
G	TYR181
G	MLI301

site_id	AC9
Number of Residues	3
Details	binding site for residue FMT G 303

Chain	Residue
G	GLN144
H	SER23
H	TYR29

site_id	AD1
Number of Residues	6
Details	binding site for residue MLI H 501

Chain	Residue
H	THR124
H	GLY125
H	ALA126
H	GLN128
H	HIS129
H	LEU180

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

Chain	Residue
H	LYS47
H	GLU48
H	ARG114
H	HOH703

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

Chain	Residue
B	LYS402
B	GLY405
B	GLY408
H	TRP403

site_id	AD4
Number of Residues	2
Details	binding site for residue FMT H 504

Chain	Residue
H	ASP337
H	GLU378

site_id	AD5
Number of Residues	6
Details	binding site for residue FMT H 505

Chain	Residue
B	HOH628
D	ARG164
D	HOH605
H	ARG355
H	PHE404
H	HOH630

site_id	AD6
Number of Residues	6
Details	binding site for residue MLI E 301

Chain	Residue
E	TYR181
E	GLY217
E	GLY219
E	GLY239
E	SER240
E	FMT303

site_id	AD7
Number of Residues	1
Details	binding site for residue FMT E 302

Chain	Residue
E	GLN144

site_id	AD8
Number of Residues	6
Details	binding site for residue FMT E 303

Chain	Residue
E	TYR30
E	GLU57
E	ILE72
E	MET106
E	TYR181
E	MLI301

site_id	AD9
Number of Residues	8
Details	binding site for residue MLI F 501

Chain	Residue
F	LLP101
F	THR124
F	GLY125
F	ALA126
F	GLN128
F	HIS129
F	LEU180
F	ALA316

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

Chain	Residue
F	LYS47
F	GLU48
F	ARG114

site_id	AE2
Number of Residues	2
Details	binding site for residue FMT F 503

Chain	Residue
D	SER84
F	ARG236

site_id	AE3
Number of Residues	5
Details	binding site for residue MLI C 301

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

site_id	AE4
Number of Residues	3
Details	binding site for residue FMT C 302

Chain	Residue
C	TYR181
C	ILE237
C	GLU57

site_id	AE5
Number of Residues	9
Details	binding site for residue MLI D 501

Chain	Residue
D	THR124
D	GLY125
D	ALA126
D	GLN128
D	HIS129
D	LEU180
D	ALA316
D	HOH653
D	HOH689

site_id	AE6
Number of Residues	4
Details	binding site for residue FMT D 502

Chain	Residue
D	ALA36
D	GLU40
D	ALA195
D	ASP196

site_id	AE7
Number of Residues	2
Details	binding site for residue FMT D 503

Chain	Residue
D	GLU48
D	ARG114

site_id	AE8
Number of Residues	4
Details	binding site for residue FMT D 504

Chain	Residue
D	HIS11
D	LEU259
D	ASP260
D	ARG335

site_id	AE9
Number of Residues	2
Details	binding site for residue FMT D 505

Chain	Residue
C	GLN144
D	SER23

site_id	AF1
Number of Residues	3
Details	binding site for residue FMT D 506

Chain	Residue
D	ARG119
D	HOH667
H	GLN80

Functional Information from PROSITE/UniProt

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

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)