3QKT

Rad50 ABC-ATPase with adjacent coiled-coil region in complex with AMP-PNP

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0016887	molecular_function	ATP hydrolysis activity
B	0016887	molecular_function	ATP hydrolysis activity
C	0016887	molecular_function	ATP hydrolysis activity
D	0016887	molecular_function	ATP hydrolysis activity

Functional Information from PDB Data

site_id	AC1
Number of Residues	31
Details	BINDING SITE FOR RESIDUE ANP A 901

Chain	Residue
A	ARG12
A	SER38
A	GLU60
A	THR62
A	LYS63
A	VAL64
A	GLN140
A	HOH314
A	HOH685
A	GLU823
A	HOH883
A	SER13
A	HOH890
A	HOH891
A	MG902
A	HOH905
B	LYS763
B	TYR764
B	PHE791
B	SER793
B	GLY794
B	GLY795
A	GLN31
B	GLU796
B	HOH892
A	ASN32
A	GLY33
A	SER34
A	GLY35
A	LYS36
A	SER37

---

site_id	AC2
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MG A 902

Chain	Residue
A	SER37
A	GLN140
A	HOH685
A	HOH883
A	ANP901

---

site_id	AC3
Number of Residues	30
Details	BINDING SITE FOR RESIDUE ANP B 901

Chain	Residue
A	LYS763
A	TYR764
A	PHE791
A	SER793
A	GLY794
A	GLY795
A	GLU796
A	HOH885
B	ARG12
B	SER13
B	GLN31
B	ASN32
B	GLY33
B	SER34
B	GLY35
B	LYS36
B	SER37
B	SER38
B	GLU60
B	THR62
B	LYS63
B	VAL64
B	GLN140
B	GLU823
B	HOH883
B	HOH889
B	HOH893
B	MG902
B	HOH918
B	HOH920

---

site_id	AC4
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MG B 902

Chain	Residue
B	SER37
B	GLN140
B	HOH684
B	HOH883
B	ANP901

---

site_id	AC5
Number of Residues	30
Details	BINDING SITE FOR RESIDUE ANP C 901

Chain	Residue
D	GLY795
D	GLU796
C	ARG12
C	SER13
C	GLN31
C	ASN32
C	GLY33
C	SER34
C	GLY35
C	LYS36
C	SER37
C	SER38
C	GLU60
C	THR62
C	LYS63
C	VAL64
C	GLN140
C	HOH184
C	HOH701
C	GLU823
C	HOH886
C	HOH894
C	MG902
C	HOH922
C	HOH924
D	LYS763
D	TYR764
D	PHE791
D	SER793
D	GLY794

---

site_id	AC6
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MG C 902

Chain	Residue
C	SER37
C	GLN140
C	HOH603
C	HOH701
C	ANP901

---

site_id	AC7
Number of Residues	30
Details	BINDING SITE FOR RESIDUE ANP D 901

Chain	Residue
C	LYS763
C	TYR764
C	PHE791
C	SER793
C	GLY794
C	GLY795
C	GLU796
C	HOH891
D	ARG12
D	SER13
D	GLN31
D	ASN32
D	GLY33
D	SER34
D	GLY35
D	LYS36
D	SER37
D	SER38
D	GLU60
D	THR62
D	LYS63
D	VAL64
D	GLN140
D	HOH189
D	GLU823
D	HOH884
D	MG902
D	HOH905
D	HOH908
D	HOH921

---

site_id	AC8
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MG D 902

Chain	Residue
D	SER37
D	GLN140
D	HOH702
D	HOH884
D	ANP901

---

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

---