3HF1

Crystal structure of human p53R2

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000731	biological_process	DNA synthesis involved in DNA repair
A	0004748	molecular_function	ribonucleoside-diphosphate reductase activity, thioredoxin disulfide as acceptor
A	0005515	molecular_function	protein binding
A	0005634	cellular_component	nucleus
A	0005654	cellular_component	nucleoplasm
A	0005737	cellular_component	cytoplasm
A	0005739	cellular_component	mitochondrion
A	0005829	cellular_component	cytosol
A	0005971	cellular_component	ribonucleoside-diphosphate reductase complex
A	0006264	biological_process	mitochondrial DNA replication
A	0006281	biological_process	DNA repair
A	0006974	biological_process	DNA damage response
A	0009185	biological_process	ribonucleoside diphosphate metabolic process
A	0009263	biological_process	deoxyribonucleotide biosynthetic process
A	0009265	biological_process	2'-deoxyribonucleotide biosynthetic process
A	0010971	biological_process	positive regulation of G2/M transition of mitotic cell cycle
A	0014075	biological_process	response to amine
A	0016491	molecular_function	oxidoreductase activity
A	0042802	molecular_function	identical protein binding
A	0046872	molecular_function	metal ion binding
A	0070318	biological_process	positive regulation of G0 to G1 transition
A	1901992	biological_process	positive regulation of mitotic cell cycle phase transition
B	0000731	biological_process	DNA synthesis involved in DNA repair
B	0004748	molecular_function	ribonucleoside-diphosphate reductase activity, thioredoxin disulfide as acceptor
B	0005515	molecular_function	protein binding
B	0005634	cellular_component	nucleus
B	0005654	cellular_component	nucleoplasm
B	0005737	cellular_component	cytoplasm
B	0005739	cellular_component	mitochondrion
B	0005829	cellular_component	cytosol
B	0005971	cellular_component	ribonucleoside-diphosphate reductase complex
B	0006264	biological_process	mitochondrial DNA replication
B	0006281	biological_process	DNA repair
B	0006974	biological_process	DNA damage response
B	0009185	biological_process	ribonucleoside diphosphate metabolic process
B	0009263	biological_process	deoxyribonucleotide biosynthetic process
B	0009265	biological_process	2'-deoxyribonucleotide biosynthetic process
B	0010971	biological_process	positive regulation of G2/M transition of mitotic cell cycle
B	0014075	biological_process	response to amine
B	0016491	molecular_function	oxidoreductase activity
B	0042802	molecular_function	identical protein binding
B	0046872	molecular_function	metal ion binding
B	0070318	biological_process	positive regulation of G0 to G1 transition
B	1901992	biological_process	positive regulation of mitotic cell cycle phase transition

Functional Information from PDB Data

site_id	AC1
Number of Residues	5
Details	BINDING SITE FOR RESIDUE FE A 401

Chain	Residue
A	GLN127
A	GLU131
A	GLU194
A	GLU228
A	HIS231

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site_id	AC2
Number of Residues	4
Details	BINDING SITE FOR RESIDUE SO4 A 502

Chain	Residue
A	TRP78
A	TYR145
A	ARG147
A	LYS151

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site_id	AC3
Number of Residues	4
Details	BINDING SITE FOR RESIDUE FE B 401

Chain	Residue
B	GLU131
B	GLU194
B	GLU228
B	HIS231

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site_id	AC4
Number of Residues	4
Details	BINDING SITE FOR RESIDUE FE B 402

Chain	Residue
B	ASP100
B	GLU131
B	HIS134
B	GLU228

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site_id	AC5
Number of Residues	1
Details	BINDING SITE FOR RESIDUE SO4 B 501

Chain	Residue
B	ARG211

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Functional Information from PROSITE/UniProt

site_id	PS00368
Number of Residues	17
Details	RIBORED_SMALL Ribonucleotide reductase small subunit signature. IEn.VHSeMYslLidtYI

Chain	Residue	Details
A	ILE130-ILE146

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	2
Details	Active site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU10014","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI2
Number of Residues	12
Details	Binding site: {}

Chain

Residue

Details

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Catalytic Information from CSA

site_id	CSA1
Number of Residues	1
Details	Annotated By Reference To The Literature 1xik

Chain	Residue	Details
A	TYR138

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site_id	CSA2
Number of Residues	1
Details	Annotated By Reference To The Literature 1xik

Chain	Residue	Details
B	TYR138

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