6EBY | pdb_00006eby

Crystal structure of the MbtH-like protein FscK bound to the interface forming region of FscH adenylation domain from Thermobifida fusca

External Resource: Annotation

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

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

Chains	Domain Info	Class	Fold	Superfamily	Family	Domain	Species	Provenance Source (Version)
C	d6ebyc_	Alpha and beta proteins (a+b)	MbtH/L9 domain-like	MbtH-like	automated matches	automated matches	(Thermobifida fusca YX ) [TaxId: 269800 ],	SCOPe (2.08)
A	d6ebya_	Alpha and beta proteins (a+b)	MbtH/L9 domain-like	MbtH-like	automated matches	automated matches	(Thermobifida fusca YX ) [TaxId: 269800 ],	SCOPe (2.08)

Domain Annotation: ECOD Classification ECOD Database Homepage

Chains	Family Name	Domain Identifier	Architecture	Possible Homology	Homology	Topology	Family	Provenance Source (Version)
D	AMP-binding_3rd	e6ebyD1	A: beta barrels	X: beta-barrel domain in acetyl-CoA synthetase-like proteins (From Topology)	H: beta-barrel domain in acetyl-CoA synthetase-like proteins (From Topology)	T: beta-barrel domain in acetyl-CoA synthetase-like proteins	F: AMP-binding_3rd	ECOD (1.6)
B	AMP-binding_3rd	e6ebyB1	A: beta barrels	X: beta-barrel domain in acetyl-CoA synthetase-like proteins (From Topology)	H: beta-barrel domain in acetyl-CoA synthetase-like proteins (From Topology)	T: beta-barrel domain in acetyl-CoA synthetase-like proteins	F: AMP-binding_3rd	ECOD (1.6)
C	MbtH	e6ebyC1	A: a+b two layers	X: L9 N-domain-like	H: MbtH-like (From Topology)	T: MbtH-like	F: MbtH	ECOD (1.6)
A	MbtH	e6ebyA1	A: a+b two layers	X: L9 N-domain-like	H: MbtH-like (From Topology)	T: MbtH-like	F: MbtH	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
D	2.30.38.10	Mainly Beta	Roll	Luciferase	domain 3	CATH (utative)
B	2.30.38.10	Mainly Beta	Roll	Luciferase	domain 3	CATH (utative)
C	3.90.820.10	Alpha Beta	Alpha-Beta Complex	Rubredoxin-like	Structural Genomics, Unknown Function 30-nov-00 1gh9 Mol_id	CATH (utative)
A	3.90.820.10	Alpha Beta	Alpha-Beta Complex	Rubredoxin-like	Structural Genomics, Unknown Function 30-nov-00 1gh9 Mol_id	CATH (utative)

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
B, D	Amino acid adenylation	vitamin binding amide binding modified amino acid binding binding phosphopantetheine binding small molecule binding catalytic activity	secondary metabolite biosynthetic process biosynthetic process metabolic process cellular process secondary metabolic process lipid biosynthetic process primary metabolic process lipid metabolic process amino acid activation peptide biosynthetic process amino acid activation for nonribosomal peptide biosynthetic process amino acid metabolic process nonribosomal peptide biosynthetic process peptide metabolic process	cellular anatomical structure intracellular anatomical structure cytoplasm cytosol
A, C	Conserved protein MbtH	-	siderophore biosynthetic process peptide biosynthetic process biosynthetic process secondary metabolite biosynthetic process siderophore metabolic process metabolic process cellular process nonribosomal peptide biosynthetic process peptide metabolic process secondary metabolic process	cellular anatomical structure intracellular anatomical structure cytoplasm cytosol

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
B, D	IPR006162	Phosphopantetheine attachment site	PTM
B, D	IPR009081	Phosphopantetheine binding ACP domain	Domain
B, D	IPR020806	Polyketide synthase-like, phosphopantetheine-binding domain	Domain
B, D	IPR010071	Amino acid adenylation domain	Domain
B, D	IPR029058	Alpha/Beta hydrolase fold	Homologous Superfamily
B, D	IPR023213	Chloramphenicol acetyltransferase-like domain superfamily	Homologous Superfamily
B, D	IPR045851	AMP-binding enzyme, C-terminal domain superfamily	Homologous Superfamily
B, D	IPR001242	Condensation domain	Domain
B, D	IPR036736	ACP-like superfamily	Homologous Superfamily
B, D	IPR025110	AMP-binding enzyme, C-terminal domain	Domain
B, D	IPR000873	AMP-dependent synthetase/ligase domain	Domain
A, C	IPR038020	MbtH-like domain superfamily	Homologous Superfamily
A, C	IPR037407	MbtH-like protein	Family
A, C	IPR005153	MbtH-like domain	Domain

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.