1II8

Crystal structure of the P. furiosus Rad50 ATPase domain

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0006302	biological_process	double-strand break repair
A	0016887	molecular_function	ATP hydrolysis activity

Functional Information from PDB Data

site_id	AC1
Number of Residues	9
Details	BINDING SITE FOR RESIDUE PO4 A 1001

Chain	Residue
A	GLN31
A	ASN32
A	GLY33
A	SER34
A	GLY35
A	LYS36
A	SER37
A	HOH1004
A	HOH1013

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site_id	AC2
Number of Residues	7
Details	BINDING SITE FOR RESIDUE PO4 A 1003

Chain	Residue
A	TRP49
A	PRO50
A	LEU51
A	ARG52
A	ILE53
A	ILE56
A	PHE61

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	11
Details	Binding site: {"evidences":[{"source":"PubMed","id":"10892749","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"21441914","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"24493214","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1F2U","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3QKT","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3QKU","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4NCJ","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI2
Number of Residues	1
Details	Binding site: {"evidences":[{"source":"PubMed","id":"10892749","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"21441914","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1F2U","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3QKT","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3QKU","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI3
Number of Residues	6
Details	Binding site: {"evidences":[{"source":"PubMed","id":"10892749","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"21441914","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1F2U","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3QKT","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

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