Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

3NMI

Crystal structure of the phenanthroline-modified cytochrome cb562 variant, MBP-Phen2

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0005506	molecular_function	iron ion binding
A	0009055	molecular_function	electron transfer activity
A	0020037	molecular_function	heme binding
A	0022900	biological_process	electron transport chain
A	0042597	cellular_component	periplasmic space
A	0046872	molecular_function	metal ion binding
B	0005506	molecular_function	iron ion binding
B	0009055	molecular_function	electron transfer activity
B	0020037	molecular_function	heme binding
B	0022900	biological_process	electron transport chain
B	0042597	cellular_component	periplasmic space
B	0046872	molecular_function	metal ion binding
C	0005506	molecular_function	iron ion binding
C	0009055	molecular_function	electron transfer activity
C	0020037	molecular_function	heme binding
C	0022900	biological_process	electron transport chain
C	0042597	cellular_component	periplasmic space
C	0046872	molecular_function	metal ion binding
D	0005506	molecular_function	iron ion binding
D	0009055	molecular_function	electron transfer activity
D	0020037	molecular_function	heme binding
D	0022900	biological_process	electron transport chain
D	0042597	cellular_component	periplasmic space
D	0046872	molecular_function	metal ion binding
E	0005506	molecular_function	iron ion binding
E	0009055	molecular_function	electron transfer activity
E	0020037	molecular_function	heme binding
E	0022900	biological_process	electron transport chain
E	0042597	cellular_component	periplasmic space
E	0046872	molecular_function	metal ion binding
F	0005506	molecular_function	iron ion binding
F	0009055	molecular_function	electron transfer activity
F	0020037	molecular_function	heme binding
F	0022900	biological_process	electron transport chain
F	0042597	cellular_component	periplasmic space
F	0046872	molecular_function	metal ion binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	15
Details	BINDING SITE FOR RESIDUE HEM A 150

Chain	Residue
A	MET7
A	HIS102
A	TYR105
A	ARG106
A	ARG106
A	HOH142
A	HOH198
A	ASN11
A	ASN11
A	LYS15
A	PRO46
A	PHE61
A	PHE65
A	CYS98
A	CYS101

site_id	AC2
Number of Residues	10
Details	BINDING SITE FOR RESIDUE PXX A 151

Chain	Residue
A	ALA43
A	PRO53
A	ASP54
A	MET58
A	CYS59
A	ALA62
A	HOH112
A	HOH128
C	GLN41
C	PXX151

site_id	AC3
Number of Residues	6
Details	BINDING SITE FOR RESIDUE ACT A 107

Chain	Residue
A	GLY64
A	THR97
A	CYS101
A	LYS104
B	LYS104
B	HOH141

site_id	AC4
Number of Residues	6
Details	BINDING SITE FOR RESIDUE ACT A 108

Chain	Residue
A	ASN11
A	LYS15
A	GLU18
A	LYS95
A	ARG106
A	HOH142

site_id	AC5
Number of Residues	17
Details	BINDING SITE FOR RESIDUE HEM B 150

Chain	Residue
B	MET7
B	ASN11
B	ASN11
B	LYS15
B	MET33
B	PRO45
B	PRO46
B	PHE61
B	PHE65
B	CYS98
B	CYS101
B	HIS102
B	TYR105
B	ARG106
B	HOH110
B	HOH164
B	HOH171

site_id	AC6
Number of Residues	9
Details	BINDING SITE FOR RESIDUE PXX B 151

Chain	Residue
B	ALA43
B	PRO53
B	ASP54
B	MET58
B	CYS59
B	ALA62
B	HOH127
F	GLN41
F	PXX151

site_id	AC7
Number of Residues	15
Details	BINDING SITE FOR RESIDUE HEM C 150

Chain	Residue
C	GLU4
C	MET7
C	PRO45
C	PRO46
C	PHE61
C	PHE65
C	CYS98
C	CYS101
C	HIS102
C	TYR105
C	ARG106
C	HOH122
D	ASN11
D	LYS15
D	ARG106

site_id	AC8
Number of Residues	11
Details	BINDING SITE FOR RESIDUE PXX C 151

Chain	Residue
A	GLN41
A	PXX151
C	GLN41
C	LYS42
C	ALA43
C	PRO53
C	ASP54
C	MET58
C	CYS59
C	ALA62
C	HOH121

site_id	AC9
Number of Residues	5
Details	BINDING SITE FOR RESIDUE ACT C 107

Chain	Residue
C	ASN99
C	HIS102
D	HIS102
D	ARG106
D	HOH108

site_id	BC1
Number of Residues	12
Details	BINDING SITE FOR RESIDUE HEM D 150

Chain	Residue
D	PHE65
D	THR97
D	CYS98
D	CYS101
D	HIS102
D	TYR105
D	ARG106
C	ASN11
C	LYS15
D	MET7
D	PRO45
D	PHE61

site_id	BC2
Number of Residues	3
Details	BINDING SITE FOR RESIDUE PXX D 151

Chain	Residue
D	CYS59
E	CYS59
E	PXX151

site_id	BC3
Number of Residues	16
Details	BINDING SITE FOR RESIDUE HEM E 150

Chain	Residue
E	GLU4
E	MET7
E	PRO45
E	PRO46
E	PHE61
E	PHE65
E	THR97
E	CYS98
E	CYS101
E	HIS102
E	TYR105
E	ARG106
E	HOH240
F	ASN11
F	LYS15
F	ARG106

site_id	BC4
Number of Residues	5
Details	BINDING SITE FOR RESIDUE PXX E 151

Chain	Residue
D	PXX151
E	GLN41
E	CYS59
E	ALA62
E	ALA66

site_id	BC5
Number of Residues	8
Details	BINDING SITE FOR RESIDUE ACT E 107

Chain	Residue
C	THR96
C	HOH109
D	GLN103
E	LYS95
E	THR96
E	HOH114
E	HOH181
F	GLN103

site_id	BC6
Number of Residues	5
Details	BINDING SITE FOR RESIDUE ACT E 108

Chain	Residue
E	ASN99
E	HIS102
E	HOH183
F	HIS102
F	ARG106

site_id	BC7
Number of Residues	11
Details	BINDING SITE FOR RESIDUE HEM F 150

Chain	Residue
E	ASN11
E	LYS15
F	MET7
F	ASN11
F	PRO46
F	PHE61
F	CYS98
F	CYS101
F	HIS102
F	TYR105
F	ARG106

site_id	BC8
Number of Residues	9
Details	BINDING SITE FOR RESIDUE PXX F 151

Chain	Residue
B	GLN41
B	ALA62
B	PXX151
F	ALA43
F	PRO53
F	MET58
F	CYS59
F	ALA62
F	HOH110

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	12
Details	BINDING: axial binding residue

Chain	Residue	Details
A	MET7
E	HIS102
F	MET7
F	HIS102
A	HIS102
B	MET7
B	HIS102
C	MET7
C	HIS102
D	MET7
D	HIS102
E	MET7

		Sequence (fasta)
		PDBx/mmCIF
		PDBML format (no-atom)
		PDB format (full)
		Validation report (PDF)
		EDMap 2fo-fc (MTZ)