4NCJ

Crystal Structure of Pyrococcus furiosis Rad50 R805E mutation with ADP Beryllium Flouride

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
C	0006302	biological_process	double-strand break repair
C	0016887	molecular_function	ATP hydrolysis activity
D	0006302	biological_process	double-strand break repair
D	0016887	molecular_function	ATP hydrolysis activity

Functional Information from PDB Data

site_id	AC1
Number of Residues	24
Details	BINDING SITE FOR RESIDUE ADP A 901

Chain	Residue
A	ARG12
A	THR62
A	LYS63
A	VAL64
A	BEF902
A	MG903
A	HOH1011
A	HOH1018
A	HOH1045
A	HOH1046
A	HOH1070
A	SER13
C	LYS763
C	TYR764
C	PHE791
C	SER793
C	GLU796
A	GLY33
A	SER34
A	GLY35
A	LYS36
A	SER37
A	SER38
A	GLU60

---

site_id	AC2
Number of Residues	11
Details	BINDING SITE FOR RESIDUE BEF A 902

Chain	Residue
A	ASN32
A	GLY33
A	LYS36
A	GLN140
A	ADP901
A	MG903
A	HOH1003
A	HOH1053
C	SER793
C	GLY794
C	GLY795

---

site_id	AC3
Number of Residues	6
Details	BINDING SITE FOR RESIDUE MG A 903

Chain	Residue
A	SER37
A	GLN140
A	ADP901
A	BEF902
A	HOH1045
A	HOH1053

---

site_id	AC4
Number of Residues	25
Details	BINDING SITE FOR RESIDUE ADP B 901

Chain	Residue
B	ARG12
B	SER13
B	ASN32
B	GLY33
B	SER34
B	GLY35
B	LYS36
B	SER37
B	SER38
B	GLU60
B	THR62
B	LYS63
B	VAL64
B	BEF902
B	MG903
B	HOH1003
B	HOH1007
B	HOH1043
B	HOH1046
B	HOH1071
D	LYS763
D	TYR764
D	PHE791
D	SER793
D	GLU796

---

site_id	AC5
Number of Residues	12
Details	BINDING SITE FOR RESIDUE BEF B 902

Chain	Residue
B	ASN32
B	GLY33
B	LYS36
B	GLN140
B	ADP901
B	MG903
B	HOH1003
B	HOH1012
B	HOH1065
D	SER793
D	GLY794
D	GLY795

---

site_id	AC6
Number of Residues	6
Details	BINDING SITE FOR RESIDUE MG B 903

Chain	Residue
B	SER37
B	GLN140
B	ADP901
B	BEF902
B	HOH1003
B	HOH1065

---

site_id	AC7
Number of Residues	26
Details	BINDING SITE FOR RESIDUE ADP C 901

Chain	Residue
C	THR62
C	LYS63
C	VAL64
C	BEF902
C	MG903
C	HOH1001
C	HOH1002
C	HOH1030
C	HOH1045
C	HOH1053
C	HOH1080
A	LYS763
A	TYR764
A	PHE791
A	SER793
A	GLU796
C	ARG12
C	SER13
C	ASN32
C	GLY33
C	SER34
C	GLY35
C	LYS36
C	SER37
C	SER38
C	GLU60

---

site_id	AC8
Number of Residues	12
Details	BINDING SITE FOR RESIDUE BEF C 902

Chain	Residue
A	SER793
A	GLY794
A	GLY795
A	HOH1083
C	ASN32
C	GLY33
C	LYS36
C	GLN140
C	ADP901
C	MG903
C	HOH1002
C	HOH1023

---

site_id	AC9
Number of Residues	6
Details	BINDING SITE FOR RESIDUE MG C 903

Chain	Residue
C	SER37
C	GLN140
C	ADP901
C	BEF902
C	HOH1001
C	HOH1002

---

site_id	BC1
Number of Residues	26
Details	BINDING SITE FOR RESIDUE ADP D 901

Chain	Residue
B	LYS763
B	TYR764
B	PHE791
B	SER793
B	GLU796
D	ARG12
D	SER13
D	ASN32
D	GLY33
D	SER34
D	GLY35
D	LYS36
D	SER37
D	SER38
D	GLU60
D	THR62
D	LYS63
D	VAL64
D	BEF902
D	MG903
D	HOH1004
D	HOH1005
D	HOH1028
D	HOH1035
D	HOH1058
D	HOH1059

---

site_id	BC2
Number of Residues	13
Details	BINDING SITE FOR RESIDUE BEF D 902

Chain	Residue
B	SER793
B	GLY794
B	GLY795
D	ASN32
D	GLY33
D	LYS36
D	GLN140
D	ADP901
D	MG903
D	HOH1004
D	HOH1005
D	HOH1024
D	HOH1086

---

site_id	BC3
Number of Residues	6
Details	BINDING SITE FOR RESIDUE MG D 903

Chain	Residue
D	SER37
D	GLN140
D	ADP901
D	BEF902
D	HOH1004
D	HOH1005

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	12
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
D	ARG12
D	ASN32
D	GLU60
A	ASN32
A	GLU60
B	ARG12
B	ASN32
B	GLU60
C	ARG12
C	ASN32
C	GLU60

---

site_id	SWS_FT_FI2
Number of Residues	4
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
C	GLN140
D	GLN140

---

site_id	SWS_FT_FI3
Number of Residues	8
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
C	LYS763
C	PHE791
D	LYS763
D	PHE791

---