4NCK

Crystal Structure of Pyrococcus furiosis Rad50 R797G mutation

Functional Information from GO Data

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

Functional Information from PDB Data

site_id	AC1
Number of Residues	7
Details	BINDING SITE FOR RESIDUE SO4 B 901

Chain	Residue
B	PRO50
B	LEU51
B	ARG52
B	ILE53
B	ILE56
B	LYS57
B	LYS58

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site_id	AC2
Number of Residues	3
Details	BINDING SITE FOR RESIDUE CL B 902

Chain	Residue
B	SER37
B	GLY35
B	LYS36

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site_id	AC3
Number of Residues	1
Details	BINDING SITE FOR RESIDUE MG B 903

Chain	Residue
B	GLU758

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	6
Details	BINDING: BINDING => ECO:0000269|PubMed:10892749, ECO:0000269|PubMed:21441914, ECO:0000269|PubMed:24493214, ECO:0007744|PDB:1F2U, ECO:0007744|PDB:3QKT, ECO:0007744|PDB:3QKU, ECO:0007744|PDB:4NCJ

Chain	Residue	Details
A	ARG12
A	ASN32
A	GLU60
B	ARG12
B	ASN32
B	GLU60

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site_id	SWS_FT_FI2
Number of Residues	2
Details	BINDING: BINDING => ECO:0000269|PubMed:10892749, ECO:0000269|PubMed:21441914, ECO:0007744|PDB:1F2U, ECO:0007744|PDB:3QKT, ECO:0007744|PDB:3QKU

Chain	Residue	Details
A	GLN140
B	GLN140

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site_id	SWS_FT_FI3
Number of Residues	4
Details	BINDING: BINDING => ECO:0000269|PubMed:10892749, ECO:0000269|PubMed:21441914, ECO:0007744|PDB:1F2U, ECO:0007744|PDB:3QKT

Chain	Residue	Details
A	LYS763
A	PHE791
B	LYS763
B	PHE791

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