Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

2C4K

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

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000287	molecular_function	magnesium ion binding
A	0002189	cellular_component	ribose phosphate diphosphokinase complex
A	0004749	molecular_function	ribose phosphate diphosphokinase activity
A	0004857	molecular_function	enzyme inhibitor activity
A	0005515	molecular_function	protein binding
A	0005524	molecular_function	ATP binding
A	0005737	cellular_component	cytoplasm
A	0006015	biological_process	5-phosphoribose 1-diphosphate biosynthetic process
A	0006139	biological_process	nucleobase-containing compound metabolic process
A	0006164	biological_process	purine nucleotide biosynthetic process
A	0009165	biological_process	nucleotide biosynthetic process
A	0042802	molecular_function	identical protein binding
B	0000287	molecular_function	magnesium ion binding
B	0002189	cellular_component	ribose phosphate diphosphokinase complex
B	0004749	molecular_function	ribose phosphate diphosphokinase activity
B	0004857	molecular_function	enzyme inhibitor activity
B	0005515	molecular_function	protein binding
B	0005524	molecular_function	ATP binding
B	0005737	cellular_component	cytoplasm
B	0006015	biological_process	5-phosphoribose 1-diphosphate biosynthetic process
B	0006139	biological_process	nucleobase-containing compound metabolic process
B	0006164	biological_process	purine nucleotide biosynthetic process
B	0009165	biological_process	nucleotide biosynthetic process
B	0042802	molecular_function	identical protein binding
C	0000287	molecular_function	magnesium ion binding
C	0002189	cellular_component	ribose phosphate diphosphokinase complex
C	0004749	molecular_function	ribose phosphate diphosphokinase activity
C	0004857	molecular_function	enzyme inhibitor activity
C	0005515	molecular_function	protein binding
C	0005524	molecular_function	ATP binding
C	0005737	cellular_component	cytoplasm
C	0006015	biological_process	5-phosphoribose 1-diphosphate biosynthetic process
C	0006139	biological_process	nucleobase-containing compound metabolic process
C	0006164	biological_process	purine nucleotide biosynthetic process
C	0009165	biological_process	nucleotide biosynthetic process
C	0042802	molecular_function	identical protein binding
D	0000287	molecular_function	magnesium ion binding
D	0002189	cellular_component	ribose phosphate diphosphokinase complex
D	0004749	molecular_function	ribose phosphate diphosphokinase activity
D	0004857	molecular_function	enzyme inhibitor activity
D	0005515	molecular_function	protein binding
D	0005524	molecular_function	ATP binding
D	0005737	cellular_component	cytoplasm
D	0006015	biological_process	5-phosphoribose 1-diphosphate biosynthetic process
D	0006139	biological_process	nucleobase-containing compound metabolic process
D	0006164	biological_process	purine nucleotide biosynthetic process
D	0009165	biological_process	nucleotide biosynthetic process
D	0042802	molecular_function	identical protein binding
E	0000287	molecular_function	magnesium ion binding
E	0002189	cellular_component	ribose phosphate diphosphokinase complex
E	0004749	molecular_function	ribose phosphate diphosphokinase activity
E	0004857	molecular_function	enzyme inhibitor activity
E	0005515	molecular_function	protein binding
E	0005524	molecular_function	ATP binding
E	0005737	cellular_component	cytoplasm
E	0006015	biological_process	5-phosphoribose 1-diphosphate biosynthetic process
E	0006139	biological_process	nucleobase-containing compound metabolic process
E	0006164	biological_process	purine nucleotide biosynthetic process
E	0009165	biological_process	nucleotide biosynthetic process
E	0042802	molecular_function	identical protein binding
F	0000287	molecular_function	magnesium ion binding
F	0002189	cellular_component	ribose phosphate diphosphokinase complex
F	0004749	molecular_function	ribose phosphate diphosphokinase activity
F	0004857	molecular_function	enzyme inhibitor activity
F	0005515	molecular_function	protein binding
F	0005524	molecular_function	ATP binding
F	0005737	cellular_component	cytoplasm
F	0006015	biological_process	5-phosphoribose 1-diphosphate biosynthetic process
F	0006139	biological_process	nucleobase-containing compound metabolic process
F	0006164	biological_process	purine nucleotide biosynthetic process
F	0009165	biological_process	nucleotide biosynthetic process
F	0042802	molecular_function	identical protein binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	5
Details	BINDING SITE FOR RESIDUE SO4 B1351

Chain	Residue
A	SER344
A	MET345
B	SER54
B	ARG56
E	ARG110

site_id	AC2
Number of Residues	5
Details	BINDING SITE FOR RESIDUE SO4 B1352

Chain	Residue
E	ARG56
B	ARG110
B	SER344
B	MET345
E	SER54

site_id	AC3
Number of Residues	7
Details	BINDING SITE FOR RESIDUE SO4 C1351

Chain	Residue
C	ARG110
C	GLU343
C	SER344
C	MET345
F	SER54
F	VAL55
F	ARG56

site_id	AC4
Number of Residues	5
Details	BINDING SITE FOR RESIDUE SO4 D1351

Chain	Residue
C	SER54
C	ARG56
D	SER344
D	MET345
F	ARG110

site_id	AC5
Number of Residues	5
Details	BINDING SITE FOR RESIDUE SO4 E1351

Chain	Residue
A	SER54
A	ARG56
A	ARG110
E	SER344
E	MET345

site_id	AC6
Number of Residues	1
Details	BINDING SITE FOR RESIDUE SO4 E1352

Chain	Residue
E	ARG90

site_id	AC7
Number of Residues	5
Details	BINDING SITE FOR RESIDUE SO4 F1351

Chain	Residue
D	SER54
D	ARG56
D	ARG110
F	SER344
F	MET345

site_id	AC8
Number of Residues	5
Details	BINDING SITE FOR RESIDUE TAM B1353

Chain	Residue
B	ARG25
B	TYR160
B	LYS324
B	THR325
B	ASP327

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	6
Details	MOD_RES: N-acetylmethionine => ECO:0007744\|PubMed:19413330

Chain	Residue	Details
A	PHE1
B	PHE1
C	PHE1
D	PHE1
E	PHE1
F	PHE1

site_id	SWS_FT_FI2
Number of Residues	6
Details	MOD_RES: Phosphoserine => ECO:0007744\|PubMed:23186163

Chain	Residue	Details
A	SER177
B	SER177
C	SER177
D	SER177
E	SER177
F	SER177

site_id	SWS_FT_FI3
Number of Residues	6
Details	MOD_RES: Phosphoserine => ECO:0007744\|PubMed:18669648, ECO:0007744\|PubMed:24275569

Chain	Residue	Details
A	SER215
B	SER215
C	SER215
D	SER215
E	SER215
F	SER215

		Sequence (fasta)
		PDBx/mmCIF
		PDBML format (no-atom)
		PDB format (full)
		Validation report (PDF)
		EDMap 2fo-fc (MTZ)