6AM8

Engineered tryptophan synthase b-subunit from Pyrococcus furiosus, PfTrpB2B9 with Trp bound as E(Aex2)

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)
B	d6am8b_	Alpha and beta proteins (a/b)	Tryptophan synthase beta subunit-like PLP-dependent enzymes	Tryptophan synthase beta subunit-like PLP-dependent enzymes	Tryptophan synthase beta subunit-like PLP-dependent enzymes	automated matches	(Pyrococcus furiosus DSM 3638 ) [TaxId: 186497 ],	SCOPe (2.08)
C	d6am8c_	Alpha and beta proteins (a/b)	Tryptophan synthase beta subunit-like PLP-dependent enzymes	Tryptophan synthase beta subunit-like PLP-dependent enzymes	Tryptophan synthase beta subunit-like PLP-dependent enzymes	automated matches	(Pyrococcus furiosus DSM 3638 ) [TaxId: 186497 ],	SCOPe (2.08)
A	d6am8a_	Alpha and beta proteins (a/b)	Tryptophan synthase beta subunit-like PLP-dependent enzymes	Tryptophan synthase beta subunit-like PLP-dependent enzymes	Tryptophan synthase beta subunit-like PLP-dependent enzymes	automated matches	(Pyrococcus furiosus DSM 3638 ) [TaxId: 186497 ],	SCOPe (2.08)
D	d6am8d_	Alpha and beta proteins (a/b)	Tryptophan synthase beta subunit-like PLP-dependent enzymes	Tryptophan synthase beta subunit-like PLP-dependent enzymes	Tryptophan synthase beta subunit-like PLP-dependent enzymes	automated matches	(Pyrococcus furiosus DSM 3638 ) [TaxId: 186497 ],	SCOPe (2.08)

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
B	SCOP2B Superfamily	Tryptophan synthase beta subunit-like PLP-dependent enzymes	8033053	3001427	SCOP2B (2022-06-29)
C	SCOP2B Superfamily	Tryptophan synthase beta subunit-like PLP-dependent enzymes	8033053	3001427	SCOP2B (2022-06-29)
A	SCOP2B Superfamily	Tryptophan synthase beta subunit-like PLP-dependent enzymes	8033053	3001427	SCOP2B (2022-06-29)
D	SCOP2B Superfamily	Tryptophan synthase beta subunit-like PLP-dependent enzymes	8033053	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)
B	PALP	e6am8B1	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)
C	PALP	e6am8C2	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)
A	PALP	e6am8A2	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	PALP	e6am8D2	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)
B	3.40.50.1100	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold		CATH (4.3.0)
C	3.40.50.1100	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold		CATH (4.3.0)
A	3.40.50.1100	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold		CATH (4.3.0)
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
B, C	PF00291	Pyridoxal-phosphate dependent enzyme (PALP)	Pyridoxal-phosphate dependent enzyme	-	Family
A, 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
B, C	Tryptophan synthase beta chain 1	hydro-lyase activity lyase activity catalytic activity carbon-oxygen lyase activity tryptophan synthase activity	erythrose 4-phosphate/phosphoenolpyruvate family amino acid metabolic process aromatic amino acid metabolic process oxoacid metabolic process carboxylic acid metabolic process indole-containing compound metabolic process amino acid metabolic process primary metabolic process organic acid metabolic process alpha-amino acid metabolic process tryptophan metabolic process L-amino acid metabolic process proteinogenic amino acid metabolic process amine metabolic process indolalkylamine metabolic process erythrose 4-phosphate/phosphoenolpyruvate family amino acid metabolic process aromatic amino acid metabolic process oxoacid metabolic process carboxylic acid metabolic process indole-containing compound metabolic process amino acid metabolic process primary metabolic process organic acid metabolic process alpha-amino acid metabolic process tryptophan metabolic process L-amino acid metabolic process proteinogenic amino acid metabolic process amine metabolic process indolalkylamine metabolic process metabolic process cellular process small molecule metabolic process biogenic amine metabolic process	cellular anatomical structure intracellular anatomical structure cytoplasm
A, D	Tryptophan synthase beta chain 1	hydro-lyase activity lyase activity catalytic activity carbon-oxygen lyase activity tryptophan synthase activity	erythrose 4-phosphate/phosphoenolpyruvate family amino acid metabolic process aromatic amino acid metabolic process oxoacid metabolic process carboxylic acid metabolic process indole-containing compound metabolic process amino acid metabolic process primary metabolic process organic acid metabolic process alpha-amino acid metabolic process tryptophan metabolic process L-amino acid metabolic process proteinogenic amino acid metabolic process amine metabolic process indolalkylamine metabolic process erythrose 4-phosphate/phosphoenolpyruvate family amino acid metabolic process aromatic amino acid metabolic process oxoacid metabolic process carboxylic acid metabolic process indole-containing compound metabolic process amino acid metabolic process primary metabolic process organic acid metabolic process alpha-amino acid metabolic process tryptophan metabolic process L-amino acid metabolic process proteinogenic amino acid metabolic process amine metabolic process indolalkylamine metabolic process metabolic process cellular process small molecule metabolic process biogenic amine metabolic process	cellular anatomical structure intracellular anatomical structure cytoplasm

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
B, C	IPR023026	Tryptophan synthase beta chain/beta chain-like	Family
B, C	IPR036052	Tryptophan synthase beta chain-like, PALP domain superfamily	Homologous Superfamily
B, C	IPR006653	Tryptophan synthase, beta chain, conserved site	Conserved Site
B, C	IPR001926	Tryptophan synthase beta chain-like, PALP domain	Domain
B, C	IPR006654	Tryptophan synthase, beta chain	Family
A, D	IPR023026	Tryptophan synthase beta chain/beta chain-like	Family
A, D	IPR036052	Tryptophan synthase beta chain-like, PALP domain superfamily	Homologous Superfamily
A, D	IPR006653	Tryptophan synthase, beta chain, conserved site	Conserved Site
A, D	IPR001926	Tryptophan synthase beta chain-like, PALP domain	Domain
A, D	IPR006654	Tryptophan synthase, beta chain	Family

Protein Modification Annotation

Modified Residue(s)
Chain	Residue(s)	Description
A, 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.