4J1X

Crystal Structure of Fe(II)-HppE with alternative substrate (S)-1-HPP

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)
C	d4j1xc1	All alpha proteins	lambda repressor-like DNA-binding domains	lambda repressor-like DNA-binding domains	SinR domain-like	Hydroxypropylphosphonic acid epoxidase Fom4, N-terminal domain	(Streptomyces wedmorensis ) [TaxId: 43759 ],	SCOPe (2.08)
C	d4j1xc2	All beta proteins	Double-stranded beta-helix	RmlC-like cupins	TM1459-like	Hydroxypropylphosphonic acid epoxidase Fom4, C-terminal domain	(Streptomyces wedmorensis ) [TaxId: 43759 ],	SCOPe (2.08)
A	d4j1xa1	All alpha proteins	lambda repressor-like DNA-binding domains	lambda repressor-like DNA-binding domains	SinR domain-like	Hydroxypropylphosphonic acid epoxidase Fom4, N-terminal domain	(Streptomyces wedmorensis ) [TaxId: 43759 ],	SCOPe (2.08)
A	d4j1xa2	All beta proteins	Double-stranded beta-helix	RmlC-like cupins	TM1459-like	Hydroxypropylphosphonic acid epoxidase Fom4, C-terminal domain	(Streptomyces wedmorensis ) [TaxId: 43759 ],	SCOPe (2.08)
B	d4j1xb1	All alpha proteins	lambda repressor-like DNA-binding domains	lambda repressor-like DNA-binding domains	SinR domain-like	Hydroxypropylphosphonic acid epoxidase Fom4, N-terminal domain	(Streptomyces wedmorensis ) [TaxId: 43759 ],	SCOPe (2.08)
B	d4j1xb2	All beta proteins	Double-stranded beta-helix	RmlC-like cupins	TM1459-like	Hydroxypropylphosphonic acid epoxidase Fom4, C-terminal domain	(Streptomyces wedmorensis ) [TaxId: 43759 ],	SCOPe (2.08)

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
C	SCOP2B Superfamily	lambda C1 repressor DNA-binding domain-like	8038373	3000119	SCOP2B (2022-06-29)
C	SCOP2B Superfamily	RmlC-like cupins	8038374	3001825	SCOP2B (2022-06-29)
A	SCOP2B Superfamily	lambda C1 repressor DNA-binding domain-like	8038373	3000119	SCOP2B (2022-06-29)
A	SCOP2B Superfamily	RmlC-like cupins	8038374	3001825	SCOP2B (2022-06-29)
B	SCOP2B Superfamily	lambda C1 repressor DNA-binding domain-like	8038373	3000119	SCOP2B (2022-06-29)
B	SCOP2B Superfamily	RmlC-like cupins	8038374	3001825	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)
C	Cupin_2	e4j1xC1	A: beta sandwiches	X: jelly-roll	H: Double-stranded beta-helix (From Topology)	T: Double-stranded beta-helix	F: Cupin_2	ECOD (1.6)
C	HTH_3	e4j1xC2	A: alpha arrays	X: HTH	H: HTH	T: tetra-helical, lambda repressor-like	F: HTH_3	ECOD (1.6)
A	Cupin_2	e4j1xA1	A: beta sandwiches	X: jelly-roll	H: Double-stranded beta-helix (From Topology)	T: Double-stranded beta-helix	F: Cupin_2	ECOD (1.6)
A	HTH_3	e4j1xA2	A: alpha arrays	X: HTH	H: HTH	T: tetra-helical, lambda repressor-like	F: HTH_3	ECOD (1.6)
B	Cupin_2	e4j1xB1	A: beta sandwiches	X: jelly-roll	H: Double-stranded beta-helix (From Topology)	T: Double-stranded beta-helix	F: Cupin_2	ECOD (1.6)
B	HTH_3	e4j1xB2	A: alpha arrays	X: HTH	H: HTH	T: tetra-helical, lambda repressor-like	F: HTH_3	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
C	1.10.260.40	Mainly Alpha	Orthogonal Bundle	434 Repressor (Amino-terminal Domain)	lambda repressor-like DNA-binding domains	CATH (4.3.0)
C	2.60.120.10	Mainly Beta	Sandwich	Jelly Rolls	Jelly Rolls	CATH (4.3.0)
A	1.10.260.40	Mainly Alpha	Orthogonal Bundle	434 Repressor (Amino-terminal Domain)	lambda repressor-like DNA-binding domains	CATH (4.3.0)
A	2.60.120.10	Mainly Beta	Sandwich	Jelly Rolls	Jelly Rolls	CATH (4.3.0)
B	1.10.260.40	Mainly Alpha	Orthogonal Bundle	434 Repressor (Amino-terminal Domain)	lambda repressor-like DNA-binding domains	CATH (4.3.0)
B	2.60.120.10	Mainly Beta	Sandwich	Jelly Rolls	Jelly Rolls	CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A, B, C	PF07883	Cupin domain (Cupin_2)	Cupin domain	This family represents the conserved barrel domain of the 'cupin' superfamily [1] ('cupa' is the Latin term for a small barrel).	Domain
A, B, C	PF01381	Helix-turn-helix (HTH_3)	Helix-turn-helix	This large family of DNA binding helix-turn helix proteins includes Cro Swiss:P03036 and CI Swiss:P03034. Within the protein Swiss:Q5F9C2, the full protein fold incorporates a helix-turn-helix motif, but the function of this member is unlikely to be ...	This large family of DNA binding helix-turn helix proteins includes Cro Swiss:P03036 and CI Swiss:P03034. Within the protein Swiss:Q5F9C2, the full protein fold incorporates a helix-turn-helix motif, but the function of this member is unlikely to be that of a DNA-binding regulator, the function of most other members, so is not necessarily characteristic of the whole family [1].	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, B, C	Epoxidase	DNA binding binding organic cyclic compound binding nucleic acid binding oxidoreductase activity oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen oxidoreductase activity, acting on paired donors, with oxidation of a pair of donors resulting in the reduction of molecular oxygen to two molecules of water catalytic activity cation binding transition metal ion binding iron ion binding ion binding ferrous iron binding metal ion binding DNA binding binding organic cyclic compound binding nucleic acid binding oxidoreductase activity oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen oxidoreductase activity, acting on paired donors, with oxidation of a pair of donors resulting in the reduction of molecular oxygen to two molecules of water catalytic activity cation binding transition metal ion binding iron ion binding ion binding ferrous iron binding metal ion binding small molecule binding dioxygenase activity	antibiotic metabolic process biosynthetic process metabolic process cellular process antibiotic biosynthetic process protein-containing complex organization protein homotetramerization cellular component organization cellular component biogenesis cellular component assembly protein complex oligomerization protein tetramerization protein-containing complex assembly protein homooligomerization antibiotic metabolic process biosynthetic process metabolic process cellular process antibiotic biosynthetic process protein-containing complex organization protein homotetramerization cellular component organization cellular component biogenesis cellular component assembly protein complex oligomerization protein tetramerization protein-containing complex assembly protein homooligomerization cellular component organization or biogenesis phosphinothricin metabolic process phosphinothricin biosynthetic process	-

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B, C	IPR001387	Cro/C1-type helix-turn-helix domain	Domain
A, B, C	IPR013096	Cupin 2, conserved barrel	Domain
A, B, C	IPR010982	Lambda repressor-like, DNA-binding domain superfamily	Homologous Superfamily
A, B, C	IPR014710	RmlC-like jelly roll fold	Homologous Superfamily
A, B, C	IPR011051	RmlC-like cupin domain superfamily	Homologous Superfamily
A, B, C	IPR050807	Bacterial Transcriptional Regulators and Dioxygenases	Family

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.