2I6E

Crystal structure of protein DR0370 from Deinococcus radiodurans, Pfam DUF178

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	d2i6ea1	Alpha and beta proteins (a/b)	Periplasmic binding protein-like II	Periplasmic binding protein-like II	Phosphate binding protein-like	Hypothetical protein DR0370	(Deinococcus radiodurans ) [TaxId: 1299 ],	SCOPe (2.08)
B	d2i6eb_	Alpha and beta proteins (a/b)	Periplasmic binding protein-like II	Periplasmic binding protein-like II	Phosphate binding protein-like	Hypothetical protein DR0370	(Deinococcus radiodurans ) [TaxId: 1299 ],	SCOPe (2.08)
C	d2i6ec_	Alpha and beta proteins (a/b)	Periplasmic binding protein-like II	Periplasmic binding protein-like II	Phosphate binding protein-like	Hypothetical protein DR0370	(Deinococcus radiodurans ) [TaxId: 1299 ],	SCOPe (2.08)
D	d2i6ed_	Alpha and beta proteins (a/b)	Periplasmic binding protein-like II	Periplasmic binding protein-like II	Phosphate binding protein-like	Hypothetical protein DR0370	(Deinococcus radiodurans ) [TaxId: 1299 ],	SCOPe (2.08)
E	d2i6ee_	Alpha and beta proteins (a/b)	Periplasmic binding protein-like II	Periplasmic binding protein-like II	Phosphate binding protein-like	Hypothetical protein DR0370	(Deinococcus radiodurans ) [TaxId: 1299 ],	SCOPe (2.08)
F	d2i6ef_	Alpha and beta proteins (a/b)	Periplasmic binding protein-like II	Periplasmic binding protein-like II	Phosphate binding protein-like	Hypothetical protein DR0370	(Deinococcus radiodurans ) [TaxId: 1299 ],	SCOPe (2.08)
G	d2i6eg_	Alpha and beta proteins (a/b)	Periplasmic binding protein-like II	Periplasmic binding protein-like II	Phosphate binding protein-like	Hypothetical protein DR0370	(Deinococcus radiodurans ) [TaxId: 1299 ],	SCOPe (2.08)
H	d2i6eh_	Alpha and beta proteins (a/b)	Periplasmic binding protein-like II	Periplasmic binding protein-like II	Phosphate binding protein-like	Hypothetical protein DR0370	(Deinococcus radiodurans ) [TaxId: 1299 ],	SCOPe (2.08)

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
A	SCOP2 Family	Phosphate binding protein-like	8022012	4000229	SCOP2 (2022-06-29)
A	SCOP2 Superfamily	Type 2 solute binding protein-like	8034392	3000083	SCOP2 (2022-06-29)
B	SCOP2B Superfamily	Type 2 solute binding protein-like	8034392	3000083	SCOP2B (2022-06-29)
C	SCOP2B Superfamily	Type 2 solute binding protein-like	8034392	3000083	SCOP2B (2022-06-29)
D	SCOP2B Superfamily	Type 2 solute binding protein-like	8034392	3000083	SCOP2B (2022-06-29)
E	SCOP2B Superfamily	Type 2 solute binding protein-like	8034392	3000083	SCOP2B (2022-06-29)
F	SCOP2B Superfamily	Type 2 solute binding protein-like	8034392	3000083	SCOP2B (2022-06-29)
G	SCOP2B Superfamily	Type 2 solute binding protein-like	8034392	3000083	SCOP2B (2022-06-29)
H	SCOP2B Superfamily	Type 2 solute binding protein-like	8034392	3000083	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	VitK2_biosynth_2nd	e2i6eA3	A: a/b three-layered sandwiches	X: Periplasmic binding protein-like II (From Topology)	H: Periplasmic binding protein-like II (From Topology)	T: Periplasmic binding protein-like II	F: VitK2_biosynth_2nd	ECOD (1.6)
A	VitK2_biosynth_1st	e2i6eA2	A: a/b three-layered sandwiches	X: Periplasmic binding protein-like II (From Topology)	H: Periplasmic binding protein-like II (From Topology)	T: Periplasmic binding protein-like II	F: VitK2_biosynth_1st	ECOD (1.6)
B	VitK2_biosynth_2nd	e2i6eB1	A: a/b three-layered sandwiches	X: Periplasmic binding protein-like II (From Topology)	H: Periplasmic binding protein-like II (From Topology)	T: Periplasmic binding protein-like II	F: VitK2_biosynth_2nd	ECOD (1.6)
B	VitK2_biosynth_1st	e2i6eB2	A: a/b three-layered sandwiches	X: Periplasmic binding protein-like II (From Topology)	H: Periplasmic binding protein-like II (From Topology)	T: Periplasmic binding protein-like II	F: VitK2_biosynth_1st	ECOD (1.6)
C	VitK2_biosynth_2nd	e2i6eC2	A: a/b three-layered sandwiches	X: Periplasmic binding protein-like II (From Topology)	H: Periplasmic binding protein-like II (From Topology)	T: Periplasmic binding protein-like II	F: VitK2_biosynth_2nd	ECOD (1.6)
C	VitK2_biosynth_1st	e2i6eC1	A: a/b three-layered sandwiches	X: Periplasmic binding protein-like II (From Topology)	H: Periplasmic binding protein-like II (From Topology)	T: Periplasmic binding protein-like II	F: VitK2_biosynth_1st	ECOD (1.6)
D	VitK2_biosynth_2nd	e2i6eD1	A: a/b three-layered sandwiches	X: Periplasmic binding protein-like II (From Topology)	H: Periplasmic binding protein-like II (From Topology)	T: Periplasmic binding protein-like II	F: VitK2_biosynth_2nd	ECOD (1.6)
D	VitK2_biosynth_1st	e2i6eD2	A: a/b three-layered sandwiches	X: Periplasmic binding protein-like II (From Topology)	H: Periplasmic binding protein-like II (From Topology)	T: Periplasmic binding protein-like II	F: VitK2_biosynth_1st	ECOD (1.6)
E	VitK2_biosynth_2nd	e2i6eE1	A: a/b three-layered sandwiches	X: Periplasmic binding protein-like II (From Topology)	H: Periplasmic binding protein-like II (From Topology)	T: Periplasmic binding protein-like II	F: VitK2_biosynth_2nd	ECOD (1.6)
E	VitK2_biosynth_1st	e2i6eE2	A: a/b three-layered sandwiches	X: Periplasmic binding protein-like II (From Topology)	H: Periplasmic binding protein-like II (From Topology)	T: Periplasmic binding protein-like II	F: VitK2_biosynth_1st	ECOD (1.6)
F	VitK2_biosynth_2nd	e2i6eF1	A: a/b three-layered sandwiches	X: Periplasmic binding protein-like II (From Topology)	H: Periplasmic binding protein-like II (From Topology)	T: Periplasmic binding protein-like II	F: VitK2_biosynth_2nd	ECOD (1.6)
F	VitK2_biosynth_1st	e2i6eF2	A: a/b three-layered sandwiches	X: Periplasmic binding protein-like II (From Topology)	H: Periplasmic binding protein-like II (From Topology)	T: Periplasmic binding protein-like II	F: VitK2_biosynth_1st	ECOD (1.6)
G	VitK2_biosynth_2nd	e2i6eG2	A: a/b three-layered sandwiches	X: Periplasmic binding protein-like II (From Topology)	H: Periplasmic binding protein-like II (From Topology)	T: Periplasmic binding protein-like II	F: VitK2_biosynth_2nd	ECOD (1.6)
G	VitK2_biosynth_1st	e2i6eG1	A: a/b three-layered sandwiches	X: Periplasmic binding protein-like II (From Topology)	H: Periplasmic binding protein-like II (From Topology)	T: Periplasmic binding protein-like II	F: VitK2_biosynth_1st	ECOD (1.6)
H	VitK2_biosynth_2nd	e2i6eH2	A: a/b three-layered sandwiches	X: Periplasmic binding protein-like II (From Topology)	H: Periplasmic binding protein-like II (From Topology)	T: Periplasmic binding protein-like II	F: VitK2_biosynth_2nd	ECOD (1.6)
H	VitK2_biosynth_1st	e2i6eH1	A: a/b three-layered sandwiches	X: Periplasmic binding protein-like II (From Topology)	H: Periplasmic binding protein-like II (From Topology)	T: Periplasmic binding protein-like II	F: VitK2_biosynth_1st	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A	3.40.190.10	Alpha Beta	3-Layer(aba) Sandwich	D-Maltodextrin-Binding Protein	domain 2	CATH (4.3.0)
B	3.40.190.10	Alpha Beta	3-Layer(aba) Sandwich	D-Maltodextrin-Binding Protein	domain 2	CATH (4.3.0)
C	3.40.190.10	Alpha Beta	3-Layer(aba) Sandwich	D-Maltodextrin-Binding Protein	domain 2	CATH (4.3.0)
D	3.40.190.10	Alpha Beta	3-Layer(aba) Sandwich	D-Maltodextrin-Binding Protein	domain 2	CATH (4.3.0)
E	3.40.190.10	Alpha Beta	3-Layer(aba) Sandwich	D-Maltodextrin-Binding Protein	domain 2	CATH (4.3.0)
F	3.40.190.10	Alpha Beta	3-Layer(aba) Sandwich	D-Maltodextrin-Binding Protein	domain 2	CATH (4.3.0)
G	3.40.190.10	Alpha Beta	3-Layer(aba) Sandwich	D-Maltodextrin-Binding Protein	domain 2	CATH (4.3.0)
H	3.40.190.10	Alpha Beta	3-Layer(aba) Sandwich	D-Maltodextrin-Binding Protein	domain 2	CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A, B, C, D, E A, B, C, D, E, F, G, H	PF02621	Menaquinone biosynthesis (VitK2_biosynth)	Menaquinone biosynthesis	This family includes two enzymes which are involved in menaquinone biosynthesis. One which catalyses the conversion of cyclic de-hypoxanthine futalosine to 1,4-dihydroxy-6-naphthoate, and one which may be involved in the conversion of chorismate to f ...	This family includes two enzymes which are involved in menaquinone biosynthesis. One which catalyses the conversion of cyclic de-hypoxanthine futalosine to 1,4-dihydroxy-6-naphthoate, and one which may be involved in the conversion of chorismate to futalosine [1]. These enzymes comprise two domains with alpha/beta structures, a large domain and a small domain. A pocket between the two domains may form the active site, a conserved histidine located within this pocket could be the catalytic base [2].	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, B, C, D, E A, B, C, D, E, F, G, H	Hypothetical protein	hydro-lyase activity lyase activity catalytic activity carbon-oxygen lyase activity	biosynthetic process small molecule biosynthetic process ketone metabolic process menaquinone metabolic process metabolic process cellular process small molecule metabolic process menaquinone biosynthetic process ketone biosynthetic process	-

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B, C, D, E A, B, C, D, E, F, G, H	IPR030868	Chorismate dehydratase	Family
A, B, C, D, E A, B, C, D, E, F, G, H	IPR003773	Menaquinone biosynthesis enzyme	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.