5TCH

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

External Resource: Annotation

Domain Annotation: SCOP/SCOPe Classification
Domain Annotation: SCOP2 Classification
Domain Annotation: ECOD Classification
Domain Annotation: CATH
Protein Family Annotation
Gene Ontology: Gene Product Annotation
InterPro: Protein Family Classification
Protein Modification Annotation

Domain Annotation: SCOP/SCOPe Classification SCOP-e Database Homepage

Chains	Domain Info	Class	Fold	Superfamily	Family	Domain	Species	Provenance Source (Version)
A	d5tcha_	Alpha and beta proteins (a/b)	TIM beta/alpha-barrel	Ribulose-phoshate binding barrel	automated matches	automated matches	(Mycobacterium tuberculosis H37Rv ) [TaxId: 83332 ],	SCOPe (2.08)
C [auth G]	d5tchg_	Alpha and beta proteins (a/b)	TIM beta/alpha-barrel	Ribulose-phoshate binding barrel	automated matches	automated matches	(Mycobacterium tuberculosis H37Rv ) [TaxId: 83332 ],	SCOPe (2.08)
G [auth C]	d5tchc_	Alpha and beta proteins (a/b)	TIM beta/alpha-barrel	Ribulose-phoshate binding barrel	automated matches	automated matches	(Mycobacterium tuberculosis H37Rv ) [TaxId: 83332 ],	SCOPe (2.08)
E	d5tche_	Alpha and beta proteins (a/b)	TIM beta/alpha-barrel	Ribulose-phoshate binding barrel	automated matches	automated matches	(Mycobacterium tuberculosis H37Rv ) [TaxId: 83332 ],	SCOPe (2.08)

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
A	SCOP2B Superfamily	Ribulose-phoshate binding barrel	8070031	3000216	SCOP2B (2022-06-29)
C [auth G]	SCOP2B Superfamily	Ribulose-phoshate binding barrel	8070031	3000216	SCOP2B (2022-06-29)
G [auth C]	SCOP2B Superfamily	Ribulose-phoshate binding barrel	8070031	3000216	SCOP2B (2022-06-29)
E	SCOP2B Superfamily	Ribulose-phoshate binding barrel	8070031	3000216	SCOP2B (2022-06-29)
B	SCOP2B Superfamily	Tryptophan synthase beta subunit-like PLP-dependent enzymes	8074367	3001427	SCOP2B (2022-06-29)
F	SCOP2B Superfamily	Tryptophan synthase beta subunit-like PLP-dependent enzymes	8074367	3001427	SCOP2B (2022-06-29)
D [auth H]	SCOP2B Superfamily	Tryptophan synthase beta subunit-like PLP-dependent enzymes	8074367	3001427	SCOP2B (2022-06-29)
H [auth D]	SCOP2B Superfamily	Tryptophan synthase beta subunit-like PLP-dependent enzymes	8074367	3001427	SCOP2B (2022-06-29)

Domain Annotation: ECOD Classification ECOD Database Homepage

Chains	Family Name	Domain Identifier	Architecture	Possible Homology	Homology	Topology	Family	Provenance Source (Version)
A	Trp_syntA	e5tchA1	A: a/b barrels	X: TIM beta/alpha-barrel	H: TIM barrels (From Topology)	T: TIM barrels	F: Trp_syntA	ECOD (1.6)
C [auth G]	Trp_syntA	e5tchG1	A: a/b barrels	X: TIM beta/alpha-barrel	H: TIM barrels (From Topology)	T: TIM barrels	F: Trp_syntA	ECOD (1.6)
G [auth C]	Trp_syntA	e5tchC1	A: a/b barrels	X: TIM beta/alpha-barrel	H: TIM barrels (From Topology)	T: TIM barrels	F: Trp_syntA	ECOD (1.6)
E	Trp_syntA	e5tchE1	A: a/b barrels	X: TIM beta/alpha-barrel	H: TIM barrels (From Topology)	T: TIM barrels	F: Trp_syntA	ECOD (1.6)
B	PALP	e5tchB1	A: a/b three-layered sandwiches	X: Rossmann-like	H: Tryptophan synthase beta subunit-like PLP-dependent enzymes (From Topology)	T: Tryptophan synthase beta subunit-like PLP-dependent enzymes	F: PALP	ECOD (1.6)
F	PALP	e5tchF1	A: a/b three-layered sandwiches	X: Rossmann-like	H: Tryptophan synthase beta subunit-like PLP-dependent enzymes (From Topology)	T: Tryptophan synthase beta subunit-like PLP-dependent enzymes	F: PALP	ECOD (1.6)
D [auth H]	PALP	e5tchH2	A: a/b three-layered sandwiches	X: Rossmann-like	H: Tryptophan synthase beta subunit-like PLP-dependent enzymes (From Topology)	T: Tryptophan synthase beta subunit-like PLP-dependent enzymes	F: PALP	ECOD (1.6)
H [auth D]	PALP	e5tchD2	A: a/b three-layered sandwiches	X: Rossmann-like	H: Tryptophan synthase beta subunit-like PLP-dependent enzymes (From Topology)	T: Tryptophan synthase beta subunit-like PLP-dependent enzymes	F: PALP	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A	3.20.20.70	Alpha Beta	Alpha-Beta Barrel	TIM Barrel	Aldolase class I	CATH (4.3.0)
C [auth G]	3.20.20.70	Alpha Beta	Alpha-Beta Barrel	TIM Barrel	Aldolase class I	CATH (4.3.0)
G [auth C]	3.20.20.70	Alpha Beta	Alpha-Beta Barrel	TIM Barrel	Aldolase class I	CATH (4.3.0)
E	3.20.20.70	Alpha Beta	Alpha-Beta Barrel	TIM Barrel	Aldolase class I	CATH (4.3.0)
B	3.40.50.1100	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold		CATH (4.3.0)
F	3.40.50.1100	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold		CATH (4.3.0)
D [auth H]	3.40.50.1100	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold		CATH (4.3.0)
H [auth D]	3.40.50.1100	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold		CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A, C [auth G], E, G [auth C]	PF00290	Tryptophan synthase alpha chain (Trp_syntA)	Tryptophan synthase alpha chain	-	Domain
B, D [auth H], F, H [auth D]	PF00291	Pyridoxal-phosphate dependent enzyme (PALP)	Pyridoxal-phosphate dependent enzyme	-	Family

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, C [auth G], E, G [auth C]	Tryptophan synthase alpha chain	hydro-lyase activity lyase activity catalytic activity carbon-oxygen lyase activity tryptophan synthase activity	oxoacid metabolic process indole-containing compound metabolic process amino acid metabolic process organic acid biosynthetic process organic acid metabolic process alpha-amino acid metabolic process carboxylic acid biosynthetic process biogenic amine biosynthetic process tryptophan biosynthetic process indole-containing compound biosynthetic process indolalkylamine metabolic process small molecule metabolic process indolalkylamine biosynthetic process aromatic amino acid family biosynthetic process oxoacid metabolic process indole-containing compound metabolic process amino acid metabolic process organic acid biosynthetic process organic acid metabolic process alpha-amino acid metabolic process carboxylic acid biosynthetic process biogenic amine biosynthetic process tryptophan biosynthetic process indole-containing compound biosynthetic process indolalkylamine metabolic process small molecule metabolic process indolalkylamine biosynthetic process aromatic amino acid family biosynthetic process aromatic amino acid metabolic process small molecule biosynthetic process carboxylic acid metabolic process primary metabolic process amine metabolic process amino acid biosynthetic process biosynthetic process amine biosynthetic process metabolic process cellular process biogenic amine metabolic process alpha-amino acid biosynthetic process erythrose 4-phosphate/phosphoenolpyruvate family amino acid metabolic process tryptophan metabolic process L-amino acid metabolic process proteinogenic amino acid metabolic process	cellular anatomical structure intracellular anatomical structure cytoplasm cytosol cell periphery plasma membrane membrane
B, D [auth H], F, H [auth D]	Tryptophan synthase beta chain	hydro-lyase activity lyase activity catalytic activity carbon-oxygen lyase activity tryptophan synthase activity	oxoacid metabolic process indole-containing compound metabolic process amino acid metabolic process organic acid biosynthetic process organic acid metabolic process alpha-amino acid metabolic process carboxylic acid biosynthetic process biogenic amine biosynthetic process tryptophan biosynthetic process indole-containing compound biosynthetic process indolalkylamine metabolic process small molecule metabolic process indolalkylamine biosynthetic process aromatic amino acid family biosynthetic process oxoacid metabolic process indole-containing compound metabolic process amino acid metabolic process organic acid biosynthetic process organic acid metabolic process alpha-amino acid metabolic process carboxylic acid biosynthetic process biogenic amine biosynthetic process tryptophan biosynthetic process indole-containing compound biosynthetic process indolalkylamine metabolic process small molecule metabolic process indolalkylamine biosynthetic process aromatic amino acid family biosynthetic process aromatic amino acid metabolic process small molecule biosynthetic process carboxylic acid metabolic process primary metabolic process amine metabolic process amino acid biosynthetic process biosynthetic process amine biosynthetic process metabolic process cellular process biogenic amine metabolic process alpha-amino acid biosynthetic process erythrose 4-phosphate/phosphoenolpyruvate family amino acid metabolic process tryptophan metabolic process L-amino acid metabolic process proteinogenic amino acid metabolic process	cellular anatomical structure intracellular anatomical structure cytoplasm

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, C [auth G], E, G [auth C]	IPR002028	Tryptophan synthase, alpha chain	Family
A, C [auth G], E, G [auth C]	IPR011060	Ribulose-phosphate binding barrel	Homologous Superfamily
A, C [auth G], E, G [auth C]	IPR018204	Tryptophan synthase, alpha chain, active site	Active Site
A, C [auth G], E, G [auth C]	IPR013785	Aldolase-type TIM barrel	Homologous Superfamily
B, D [auth H], F, H [auth D]	IPR023026	Tryptophan synthase beta chain/beta chain-like	Family
B, D [auth H], F, H [auth D]	IPR036052	Tryptophan synthase beta chain-like, PALP domain superfamily	Homologous Superfamily
B, D [auth H], F, H [auth D]	IPR006653	Tryptophan synthase, beta chain, conserved site	Conserved Site
B, D [auth H], F, H [auth D]	IPR001926	Tryptophan synthase beta chain-like, PALP domain	Domain
B, D [auth H], F, H [auth D]	IPR006654	Tryptophan synthase, beta chain	Family

Protein Modification Annotation

Modified Residue(s)
Chain	Residue(s)	Description
B, D [auth H], F, H [auth D]	LLP	Parent Component: LYS RESID: AA0119 PSI-MOD : N6-pyridoxal phosphate-L-lysine MOD:00128

RCSB PDB Core Operations are funded by the U.S. National Science Foundation (DBI-2321666), the US Department of Energy (DE-SC0019749), and the National Cancer Institute, National Institute of Allergy and Infectious Diseases, and National Institute of General Medical Sciences of the National Institutes of Health under grant R01GM157729.