5KP1

Crystal Structure of Ketosteroid Isomerase from Pseudomonas putida (pKSI) bound to Equilenin; D40N, Y16(Cl-Y)

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

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

Chains	Domain Info	Class	Fold	Superfamily	Family	Domain	Species	Provenance Source (Version)
A	d5kp1a_	Alpha and beta proteins (a+b)	Cystatin-like	NTF2-like	Ketosteroid isomerase-like	Delta-5-3-ketosteroid isomerase, steroid delta-isomerase, KSI	(Pseudomonas putida ) [TaxId: 303 ],	SCOPe (2.08)
D	d5kp1d_	Alpha and beta proteins (a+b)	Cystatin-like	NTF2-like	Ketosteroid isomerase-like	Delta-5-3-ketosteroid isomerase, steroid delta-isomerase, KSI	(Pseudomonas putida ) [TaxId: 303 ],	SCOPe (2.08)
B	d5kp1b_	Alpha and beta proteins (a+b)	Cystatin-like	NTF2-like	Ketosteroid isomerase-like	Delta-5-3-ketosteroid isomerase, steroid delta-isomerase, KSI	(Pseudomonas putida ) [TaxId: 303 ],	SCOPe (2.08)
C	d5kp1c_	Alpha and beta proteins (a+b)	Cystatin-like	NTF2-like	Ketosteroid isomerase-like	Delta-5-3-ketosteroid isomerase, steroid delta-isomerase, KSI	(Pseudomonas putida ) [TaxId: 303 ],	SCOPe (2.08)

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
A	SCOP2B Superfamily	NTF2-like	8034008	3000472	SCOP2B (2022-06-29)
D	SCOP2B Superfamily	NTF2-like	8034008	3000472	SCOP2B (2022-06-29)
B	SCOP2B Superfamily	NTF2-like	8034008	3000472	SCOP2B (2022-06-29)
C	SCOP2B Superfamily	NTF2-like	8034008	3000472	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	SnoaL_5	e5kp1A1	A: a+b two layers	X: Cystatin-like	H: NTF2-like (From Topology)	T: NTF2-like	F: SnoaL_5	ECOD (1.6)
D	SnoaL_5	e5kp1D1	A: a+b two layers	X: Cystatin-like	H: NTF2-like (From Topology)	T: NTF2-like	F: SnoaL_5	ECOD (1.6)
B	SnoaL_5	e5kp1B1	A: a+b two layers	X: Cystatin-like	H: NTF2-like (From Topology)	T: NTF2-like	F: SnoaL_5	ECOD (1.6)
C	SnoaL_5	e5kp1C1	A: a+b two layers	X: Cystatin-like	H: NTF2-like (From Topology)	T: NTF2-like	F: SnoaL_5	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A	3.10.450.50	Alpha Beta	Roll	Nuclear Transport Factor 2	Chain: A,	CATH (4.3.0)
D	3.10.450.50	Alpha Beta	Roll	Nuclear Transport Factor 2	Chain: A,	CATH (4.3.0)
B	3.10.450.50	Alpha Beta	Roll	Nuclear Transport Factor 2	Chain: A,	CATH (4.3.0)
C	3.10.450.50	Alpha Beta	Roll	Nuclear Transport Factor 2	Chain: A,	CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A, B, C, D	PF12680	SnoaL-like domain (SnoaL_2)	SnoaL-like domain	This family contains a large number of proteins that share the SnoaL fold.	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, B, C, D	Steroid Delta-isomerase	isomerase activity intramolecular oxidoreductase activity, transposing C=C bonds steroid delta-isomerase activity intramolecular oxidoreductase activity catalytic activity	steroid metabolic process primary metabolic process metabolic process cellular process lipid metabolic process	-

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B, C, D	IPR032710	NTF2-like domain superfamily	Homologous Superfamily
A, B, C, D	IPR039256	Ketosteroid isomerase	Family
A, B, C, D	IPR037401	SnoaL-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.