Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

6NLG

1.50 A resolution structure of BfrB (C89S/K96C) from Pseudomonas aeruginosa in complex with a small molecule fragment (analog 1)

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004322	molecular_function	ferroxidase activity
A	0005506	molecular_function	iron ion binding
A	0005829	cellular_component	cytosol
A	0006826	biological_process	iron ion transport
A	0006879	biological_process	intracellular iron ion homeostasis
A	0006880	biological_process	intracellular sequestering of iron ion
A	0008199	molecular_function	ferric iron binding
A	0020037	molecular_function	heme binding
A	0046872	molecular_function	metal ion binding
A	0070288	cellular_component	ferritin complex
B	0004322	molecular_function	ferroxidase activity
B	0005506	molecular_function	iron ion binding
B	0005829	cellular_component	cytosol
B	0006826	biological_process	iron ion transport
B	0006879	biological_process	intracellular iron ion homeostasis
B	0006880	biological_process	intracellular sequestering of iron ion
B	0008199	molecular_function	ferric iron binding
B	0020037	molecular_function	heme binding
B	0046872	molecular_function	metal ion binding
B	0070288	cellular_component	ferritin complex
C	0004322	molecular_function	ferroxidase activity
C	0005506	molecular_function	iron ion binding
C	0005829	cellular_component	cytosol
C	0006826	biological_process	iron ion transport
C	0006879	biological_process	intracellular iron ion homeostasis
C	0006880	biological_process	intracellular sequestering of iron ion
C	0008199	molecular_function	ferric iron binding
C	0020037	molecular_function	heme binding
C	0046872	molecular_function	metal ion binding
C	0070288	cellular_component	ferritin complex
D	0004322	molecular_function	ferroxidase activity
D	0005506	molecular_function	iron ion binding
D	0005829	cellular_component	cytosol
D	0006826	biological_process	iron ion transport
D	0006879	biological_process	intracellular iron ion homeostasis
D	0006880	biological_process	intracellular sequestering of iron ion
D	0008199	molecular_function	ferric iron binding
D	0020037	molecular_function	heme binding
D	0046872	molecular_function	metal ion binding
D	0070288	cellular_component	ferritin complex

Functional Information from PDB Data

site_id	AC1
Number of Residues	5
Details	binding site for residue KT7 A 201

Chain	Residue
A	PRO69
A	LEU71
A	GLN72
B	LEU27
B	ILE79

site_id	AC2
Number of Residues	17
Details	binding site for residue HEM A 202

Chain	Residue
A	ILE49
A	MET52
A	HOH310
A	HOH314
A	HOH321
B	LEU19
B	ILE22
B	ASN23
B	PHE26
B	TYR45
B	ILE49
B	MET52
B	LYS53
A	LEU19
A	ILE22
A	ASN23
A	TYR45

site_id	AC3
Number of Residues	6
Details	binding site for residue MPD A 203

Chain	Residue
A	LYS2
A	GLY3
A	VAL111
A	ASP113
A	HOH322
D	ARG102

site_id	AC4
Number of Residues	3
Details	binding site for residue SO4 A 204

Chain	Residue
A	ARG61
A	PHE64
A	HOH318

site_id	AC5
Number of Residues	4
Details	binding site for residue SO4 A 205

Chain	Residue
A	ARG39
A	HIS43
A	HOH302
A	HOH383

site_id	AC6
Number of Residues	3
Details	binding site for residue SO4 A 206

Chain	Residue
A	GLN9
A	GLN110
A	HOH306

site_id	AC7
Number of Residues	1
Details	binding site for residue SO4 A 207

Chain	Residue
A	HIS10

site_id	AC8
Number of Residues	8
Details	binding site for residue K B 201

Chain	Residue
A	ASN148
A	GLN151
B	ASN148
B	GLN151
C	ASN148
C	GLN151
D	ASN148
D	GLN151

site_id	AC9
Number of Residues	7
Details	binding site for residue MPD B 202

Chain	Residue
B	LYS2
B	GLY3
B	ARG102
B	VAL111
B	HIS112
B	ASP113
B	HOH315

site_id	AD1
Number of Residues	6
Details	binding site for residue SO4 B 203

Chain	Residue
B	ARG117
B	ARG117
B	ASP118
B	ASP118
B	ASP118
B	HOH355

site_id	AD2
Number of Residues	3
Details	binding site for residue SO4 B 204

Chain	Residue
B	ARG61
B	PHE64
B	HOH311

site_id	AD3
Number of Residues	8
Details	binding site for residue KT7 C 201

Chain	Residue
C	LEU27
C	LEU68
C	PRO69
C	ASN70
C	LEU71
C	GLN72
C	ILE79
C	HOH303

site_id	AD4
Number of Residues	19
Details	binding site for residue HEM C 202

Chain	Residue
C	LEU19
C	ILE22
C	ASN23
C	ASN23
C	PHE26
C	PHE26
C	TYR45
C	TYR45
C	ILE49
C	ILE49
C	MET52
C	MET52
C	LYS53
C	LYS53
C	ILE59
C	HOH304
C	HOH304
C	HOH308
C	HOH308

site_id	AD5
Number of Residues	8
Details	binding site for residue MPD C 203

Chain	Residue
A	ARG102
C	LYS2
C	GLY3
C	ARG61
C	LEU65
C	VAL111
C	ASP113
C	HOH361

site_id	AD6
Number of Residues	8
Details	binding site for residue SO4 C 204

Chain	Residue
C	ARG117
C	ASP118
C	LYS121
C	HOH340
C	HOH399
D	ARG117
D	HOH392
A	ARG117

site_id	AD7
Number of Residues	3
Details	binding site for residue SO4 C 205

Chain	Residue
C	ARG61
C	PHE64
C	HOH319

site_id	AD8
Number of Residues	4
Details	binding site for residue SO4 C 206

Chain	Residue
C	ARG39
C	HIS43
C	HOH341
C	HOH377

site_id	AD9
Number of Residues	7
Details	binding site for residue KT7 D 201

Chain	Residue
D	LEU27
D	LEU68
D	PRO69
D	LEU71
D	GLN72
D	ILE79
D	HOH345

site_id	AE1
Number of Residues	16
Details	binding site for residue HEM D 202

Chain	Residue
D	LEU19
D	ILE22
D	ASN23
D	ASN23
D	PHE26
D	TYR45
D	TYR45
D	ILE49
D	ILE49
D	MET52
D	MET52
D	LYS53
D	LYS53
D	LEU71
D	HOH307
D	HOH307

site_id	AE2
Number of Residues	7
Details	binding site for residue MPD D 203

Chain	Residue
C	ARG102
D	LYS2
D	GLY3
D	VAL111
D	HIS112
D	ASP113
D	HOH323

site_id	AE3
Number of Residues	3
Details	binding site for residue SO4 D 204

Chain	Residue
D	ARG61
D	PHE64
D	HOH310

site_id	AE4
Number of Residues	4
Details	binding site for residue SO4 D 205

Chain	Residue
D	ARG39
D	HIS43
D	HOH328
D	HOH367

Functional Information from PROSITE/UniProt

site_id	PS00549
Number of Residues	19
Details	BACTERIOFERRITIN Bacterioferritin signature. MkGdkkVIqhLnkiLgneL

Chain	Residue	Details
A	MET1-LEU19

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