2C4K

Crystal structure of human phosphoribosylpyrophosphate synthetase- associated protein 39 (PAP39)

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
Pharos: Disease Associations

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

Chains	Domain Info	Class	Fold	Superfamily	Family	Domain	Species	Provenance Source (Version)
B	d2c4kb1	Alpha and beta proteins (a/b)	PRTase-like	PRTase-like	Phosphoribosylpyrophosphate synthetase-like	PRPP synthetase-associated protein 1	HUMAN (Homo sapiens ) [TaxId: 9606 ],	SCOPe (2.08)
C	d2c4kc1	Alpha and beta proteins (a/b)	PRTase-like	PRTase-like	Phosphoribosylpyrophosphate synthetase-like	PRPP synthetase-associated protein 1	HUMAN (Homo sapiens ) [TaxId: 9606 ],	SCOPe (2.08)
D	d2c4kd1	Alpha and beta proteins (a/b)	PRTase-like	PRTase-like	Phosphoribosylpyrophosphate synthetase-like	PRPP synthetase-associated protein 1	HUMAN (Homo sapiens ) [TaxId: 9606 ],	SCOPe (2.08)
F	d2c4kf1	Alpha and beta proteins (a/b)	PRTase-like	PRTase-like	Phosphoribosylpyrophosphate synthetase-like	PRPP synthetase-associated protein 1	HUMAN (Homo sapiens ) [TaxId: 9606 ],	SCOPe (2.08)
A	d2c4ka1	Alpha and beta proteins (a/b)	PRTase-like	PRTase-like	Phosphoribosylpyrophosphate synthetase-like	PRPP synthetase-associated protein 1	HUMAN (Homo sapiens ) [TaxId: 9606 ],	SCOPe (2.08)
E	d2c4ke1	Alpha and beta proteins (a/b)	PRTase-like	PRTase-like	Phosphoribosylpyrophosphate synthetase-like	PRPP synthetase-associated protein 1	HUMAN (Homo sapiens ) [TaxId: 9606 ],	SCOPe (2.08)

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
B	SCOP2B Superfamily	PRTase-like	8039325	3000060	SCOP2B (2022-06-29)
C	SCOP2B Superfamily	PRTase-like	8039325	3000060	SCOP2B (2022-06-29)
D	SCOP2B Superfamily	PRTase-like	8039325	3000060	SCOP2B (2022-06-29)
F	SCOP2B Superfamily	PRTase-like	8039325	3000060	SCOP2B (2022-06-29)
A	SCOP2 Family	Phosphoribosylpyrophosphate synthetase-like	8026946	4000640	SCOP2 (2022-06-29)
A	SCOP2 Superfamily	PRTase-like	8039326	3000060	SCOP2 (2022-06-29)
A	SCOP2 Superfamily	PRTase-like	8039325	3000060	SCOP2 (2022-06-29)
E	SCOP2B Superfamily	PRTase-like	8039325	3000060	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	Pribosyltran_N	e2c4kB1	A: a/b three-layered sandwiches	X: PRTase-like (From Topology)	H: PRTase-like (From Topology)	T: PRTase-like	F: Pribosyltran_N	ECOD (1.6)
B	Pribosyl_synth	e2c4kB2	A: a/b three-layered sandwiches	X: PRTase-like (From Topology)	H: PRTase-like (From Topology)	T: PRTase-like	F: Pribosyl_synth	ECOD (1.6)
C	Pribosyltran_N	e2c4kC1	A: a/b three-layered sandwiches	X: PRTase-like (From Topology)	H: PRTase-like (From Topology)	T: PRTase-like	F: Pribosyltran_N	ECOD (1.6)
C	Pribosyl_synth	e2c4kC2	A: a/b three-layered sandwiches	X: PRTase-like (From Topology)	H: PRTase-like (From Topology)	T: PRTase-like	F: Pribosyl_synth	ECOD (1.6)
D	Pribosyltran_N	e2c4kD1	A: a/b three-layered sandwiches	X: PRTase-like (From Topology)	H: PRTase-like (From Topology)	T: PRTase-like	F: Pribosyltran_N	ECOD (1.6)
D	Pribosyl_synth	e2c4kD2	A: a/b three-layered sandwiches	X: PRTase-like (From Topology)	H: PRTase-like (From Topology)	T: PRTase-like	F: Pribosyl_synth	ECOD (1.6)
F	Pribosyltran_N	e2c4kF1	A: a/b three-layered sandwiches	X: PRTase-like (From Topology)	H: PRTase-like (From Topology)	T: PRTase-like	F: Pribosyltran_N	ECOD (1.6)
F	Pribosyl_synth	e2c4kF2	A: a/b three-layered sandwiches	X: PRTase-like (From Topology)	H: PRTase-like (From Topology)	T: PRTase-like	F: Pribosyl_synth	ECOD (1.6)
A	Pribosyltran_N	e2c4kA1	A: a/b three-layered sandwiches	X: PRTase-like (From Topology)	H: PRTase-like (From Topology)	T: PRTase-like	F: Pribosyltran_N	ECOD (1.6)
A	Pribosyl_synth	e2c4kA2	A: a/b three-layered sandwiches	X: PRTase-like (From Topology)	H: PRTase-like (From Topology)	T: PRTase-like	F: Pribosyl_synth	ECOD (1.6)
E	Pribosyltran_N	e2c4kE1	A: a/b three-layered sandwiches	X: PRTase-like (From Topology)	H: PRTase-like (From Topology)	T: PRTase-like	F: Pribosyltran_N	ECOD (1.6)
E	Pribosyl_synth	e2c4kE2	A: a/b three-layered sandwiches	X: PRTase-like (From Topology)	H: PRTase-like (From Topology)	T: PRTase-like	F: Pribosyl_synth	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
B	3.40.50.2020	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold		CATH (4.3.0)
C	3.40.50.2020	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold		CATH (4.3.0)
D	3.40.50.2020	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold		CATH (4.3.0)
F	3.40.50.2020	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold		CATH (4.3.0)
A	3.40.50.2020	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold		CATH (4.3.0)
E	3.40.50.2020	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold		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	PF14572	Phosphoribosyl synthetase-associated domain (Pribosyl_synth)	Phosphoribosyl synthetase-associated domain	This family includes several examples of enzymes from class EC:2.7.6.1, phosphoribosyl-pyrophosphate transferase.	Domain
A, B, C, D, E A, B, C, D, E, F	PF13793	N-terminal domain of ribose phosphate pyrophosphokinase (Pribosyltran_N)	N-terminal domain of ribose phosphate pyrophosphokinase	This family is frequently found N-terminal to the Pribosyltran, Pfam:PF00156.	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	PHOSPHORIBOSYL PYROPHOSPHATE SYNTHETASE-ASSOCIATED PROTEIN 1	cation binding magnesium ion binding ion binding binding metal ion binding small molecule binding adenyl ribonucleotide binding nucleotide binding purine ribonucleotide binding purine ribonucleoside triphosphate binding nucleoside phosphate binding purine nucleotide binding organic cyclic compound binding anion binding cation binding magnesium ion binding ion binding binding metal ion binding small molecule binding adenyl ribonucleotide binding nucleotide binding purine ribonucleotide binding purine ribonucleoside triphosphate binding nucleoside phosphate binding purine nucleotide binding organic cyclic compound binding anion binding adenyl nucleotide binding ATP binding heterocyclic compound binding carbohydrate derivative binding ribonucleotide binding enzyme regulator activity molecular function inhibitor activity molecular function regulator activity enzyme inhibitor activity ribose phosphate diphosphokinase activity diphosphotransferase activity transferase activity catalytic activity transferase activity, transferring phosphorus-containing groups identical protein binding protein binding	nucleobase-containing compound metabolic process primary metabolic process metabolic process cellular process nucleoside phosphate metabolic process nucleotide biosynthetic process nucleotide metabolic process nucleobase-containing compound biosynthetic process purine-containing compound metabolic process purine nucleotide metabolic process biosynthetic process organophosphate metabolic process nucleobase-containing small molecule metabolic process organophosphate biosynthetic process nucleobase-containing compound metabolic process primary metabolic process metabolic process cellular process nucleoside phosphate metabolic process nucleotide biosynthetic process nucleotide metabolic process nucleobase-containing compound biosynthetic process purine-containing compound metabolic process purine nucleotide metabolic process biosynthetic process organophosphate metabolic process nucleobase-containing small molecule metabolic process organophosphate biosynthetic process purine-containing compound biosynthetic process phosphate-containing compound metabolic process nucleoside phosphate biosynthetic process small molecule metabolic process phosphorus metabolic process purine nucleotide biosynthetic process 5-phosphoribose 1-diphosphate biosynthetic process ribose phosphate metabolic process carbohydrate derivative biosynthetic process carbohydrate derivative metabolic process 5-phosphoribose 1-diphosphate metabolic process ribose phosphate biosynthetic process	ribose phosphate diphosphokinase complex transferase complex, transferring phosphorus-containing groups protein-containing complex catalytic complex transferase complex cellular anatomical structure intracellular anatomical structure cytoplasm

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B, C, D, E A, B, C, D, E, F	IPR029057	Phosphoribosyltransferase-like	Homologous Superfamily
A, B, C, D, E A, B, C, D, E, F	IPR029099	Ribose-phosphate pyrophosphokinase, N-terminal domain	Domain
A, B, C, D, E A, B, C, D, E, F	IPR005946	Ribose-phosphate pyrophosphokinase	Family

Pharos: Disease Associations Pharos Homepage Annotation

Chains	Drug Target	Associated Disease
A, B, C, D, E A, B, C, D, E, F	Pharos: Q14558	lung cancer medulloblastoma ovarian cancer

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.