Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

6HZ9

Structure of McrBC without DNA binding domains (Class 5)

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0005524	molecular_function	ATP binding
A	0016887	molecular_function	ATP hydrolysis activity
B	0005524	molecular_function	ATP binding
B	0016887	molecular_function	ATP hydrolysis activity
C	0005524	molecular_function	ATP binding
C	0016887	molecular_function	ATP hydrolysis activity
D	0005524	molecular_function	ATP binding
D	0016887	molecular_function	ATP hydrolysis activity
E	0005524	molecular_function	ATP binding
E	0016887	molecular_function	ATP hydrolysis activity
F	0005524	molecular_function	ATP binding
F	0016887	molecular_function	ATP hydrolysis activity
G	0005524	molecular_function	ATP binding
G	0016887	molecular_function	ATP hydrolysis activity
H	0005524	molecular_function	ATP binding
H	0016887	molecular_function	ATP hydrolysis activity
I	0005524	molecular_function	ATP binding
I	0016887	molecular_function	ATP hydrolysis activity
J	0005524	molecular_function	ATP binding
J	0016887	molecular_function	ATP hydrolysis activity
K	0005524	molecular_function	ATP binding
K	0016887	molecular_function	ATP hydrolysis activity
L	0005524	molecular_function	ATP binding
L	0016887	molecular_function	ATP hydrolysis activity
M	0005515	molecular_function	protein binding
M	0009307	biological_process	DNA restriction-modification system
M	0032067	molecular_function	type IV site-specific deoxyribonuclease activity
M	1905348	cellular_component	endonuclease complex
N	0005515	molecular_function	protein binding
N	0009307	biological_process	DNA restriction-modification system
N	0032067	molecular_function	type IV site-specific deoxyribonuclease activity
N	1905348	cellular_component	endonuclease complex

Functional Information from PDB Data

site_id	AC1
Number of Residues	19
Details	binding site for residue GNP A 1001

Chain	Residue
A	ASP176
A	GLU280
A	HIS407
A	SER408
A	CYS411
A	CYS412
A	MG1002
B	ASP300
B	LYS301
B	ARG348
B	ARG349
A	PHE178
A	PRO203
A	GLY204
A	GLY206
A	LYS207
A	THR208
A	PHE209
A	ASP279

site_id	AC2
Number of Residues	4
Details	binding site for residue MG A 1002

Chain	Residue
A	THR208
A	ASP279
A	GNP1001
B	ARG349

site_id	AC3
Number of Residues	20
Details	binding site for residue GNP B 1001

Chain	Residue
B	ASP176
B	LEU177
B	PHE178
B	PRO203
B	GLY204
B	VAL205
B	GLY206
B	LYS207
B	THR208
B	PHE209
B	GLU280
B	HIS407
B	SER408
B	CYS411
B	CYS412
B	MG1002
C	ASP300
C	LYS301
C	ARG348
C	ARG349

site_id	AC4
Number of Residues	3
Details	binding site for residue MG B 1002

Chain	Residue
B	THR208
B	GNP1001
C	ARG349

site_id	AC5
Number of Residues	20
Details	binding site for residue GNP C 1001

Chain	Residue
C	ASP176
C	LEU177
C	PHE178
C	PRO202
C	PRO203
C	GLY204
C	VAL205
C	GLY206
C	LYS207
C	THR208
C	PHE209
C	HIS407
C	SER408
C	CYS411
C	CYS412
C	MG1002
D	ASP300
D	LYS301
D	ARG348
D	ARG349

site_id	AC6
Number of Residues	2
Details	binding site for residue MG C 1002

Chain	Residue
C	THR208
C	GNP1001

site_id	AC7
Number of Residues	12
Details	binding site for residue GDP D 1001

Chain	Residue
D	ASP176
D	PHE178
D	PRO203
D	GLY204
D	VAL205
D	GLY206
D	LYS207
D	THR208
D	PHE209
D	HIS407
D	SER408
D	CYS411

site_id	AC8
Number of Residues	12
Details	binding site for residue GDP E 1001

Chain	Residue
E	ASP176
E	LEU177
E	PHE178
E	GLY204
E	VAL205
E	GLY206
E	LYS207
E	PHE209
E	HIS407
E	SER408
E	CYS412
F	ARG348

site_id	AC9
Number of Residues	11
Details	binding site for residue GDP F 1001

Chain	Residue
F	HIS407
F	SER408
F	CYS411
F	CYS412
A	ARG348
F	ASP176
F	PHE178
F	GLY206
F	LYS207
F	THR208
F	PHE209

site_id	AD1
Number of Residues	19
Details	binding site for residue GNP G 1001

Chain	Residue
G	ASP176
G	PHE178
G	PRO203
G	GLY204
G	GLY206
G	LYS207
G	THR208
G	PHE209
G	ASP279
G	GLU280
G	HIS407
G	SER408
G	CYS411
G	CYS412
G	MG1002
H	ASP300
H	LYS301
H	ARG348
H	ARG349

site_id	AD2
Number of Residues	4
Details	binding site for residue MG G 1002

Chain	Residue
G	THR208
G	ASP279
G	GNP1001
H	ARG349

site_id	AD3
Number of Residues	20
Details	binding site for residue GNP H 1001

Chain	Residue
H	ASP176
H	LEU177
H	PHE178
H	PRO203
H	GLY204
H	VAL205
H	GLY206
H	LYS207
H	THR208
H	PHE209
H	GLU280
H	HIS407
H	SER408
H	CYS411
H	CYS412
H	MG1002
I	ASP300
I	LYS301
I	ARG348
I	ARG349

site_id	AD4
Number of Residues	3
Details	binding site for residue MG H 1002

Chain	Residue
H	THR208
H	GNP1001
I	ARG349

site_id	AD5
Number of Residues	20
Details	binding site for residue GNP I 1001

Chain	Residue
I	ASP176
I	LEU177
I	PHE178
I	PRO202
I	PRO203
I	GLY204
I	VAL205
I	GLY206
I	LYS207
I	THR208
I	PHE209
I	HIS407
I	SER408
I	CYS411
I	CYS412
I	MG1002
J	ASP300
J	LYS301
J	ARG348
J	ARG349

site_id	AD6
Number of Residues	2
Details	binding site for residue MG I 1002

Chain	Residue
I	THR208
I	GNP1001

site_id	AD7
Number of Residues	12
Details	binding site for residue GDP J 1001

Chain	Residue
J	ASP176
J	PHE178
J	PRO203
J	GLY204
J	VAL205
J	GLY206
J	LYS207
J	THR208
J	PHE209
J	HIS407
J	SER408
J	CYS411

site_id	AD8
Number of Residues	13
Details	binding site for residue GDP K 1001

Chain	Residue
K	ASP176
K	LEU177
K	PHE178
K	GLY204
K	VAL205
K	GLY206
K	LYS207
K	PHE209
K	HIS407
K	SER408
K	CYS412
L	GLU298
L	ARG348

site_id	AD9
Number of Residues	11
Details	binding site for residue GDP L 1001

Chain	Residue
G	ARG348
L	ASP176
L	PHE178
L	GLY206
L	LYS207
L	THR208
L	PHE209
L	HIS407
L	SER408
L	CYS411
L	CYS412

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	36
Details	BINDING: BINDING => ECO:0000255

Chain	Residue	Details
A	GLY201
D	GLY201
D	ASP300
D	ASN333
E	GLY201
E	ASP300
E	ASN333
F	GLY201
F	ASP300
F	ASN333
G	GLY201
A	ASP300
G	ASP300
G	ASN333
H	GLY201
H	ASP300
H	ASN333
I	GLY201
I	ASP300
I	ASN333
J	GLY201
J	ASP300
A	ASN333
J	ASN333
K	GLY201
K	ASP300
K	ASN333
L	GLY201
L	ASP300
L	ASN333
B	GLY201
B	ASP300
B	ASN333
C	GLY201
C	ASP300
C	ASN333

		Sequence (fasta)
		PDBx/mmCIF
		PDBML format (no-atom)
		PDB format (full)
		Validation report (PDF)