Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

4TOF

1.65A resolution structure of BfrB (C89S, K96C) crystal form 1 from Pseudomonas aeruginosa

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004322	molecular_function	ferroxidase activity
A	0005506	molecular_function	iron ion binding
A	0005737	cellular_component	cytoplasm
A	0005829	cellular_component	cytosol
A	0006811	biological_process	monoatomic ion transport
A	0006826	biological_process	iron ion transport
A	0006879	biological_process	intracellular iron ion homeostasis
A	0008199	molecular_function	ferric iron binding
A	0016491	molecular_function	oxidoreductase activity
A	0020037	molecular_function	heme binding
A	0046872	molecular_function	metal ion binding
A	0070288	cellular_component	ferritin complex
A	0140315	molecular_function	iron ion sequestering activity
B	0004322	molecular_function	ferroxidase activity
B	0005506	molecular_function	iron ion binding
B	0005737	cellular_component	cytoplasm
B	0005829	cellular_component	cytosol
B	0006811	biological_process	monoatomic ion transport
B	0006826	biological_process	iron ion transport
B	0006879	biological_process	intracellular iron ion homeostasis
B	0008199	molecular_function	ferric iron binding
B	0016491	molecular_function	oxidoreductase activity
B	0020037	molecular_function	heme binding
B	0046872	molecular_function	metal ion binding
B	0070288	cellular_component	ferritin complex
B	0140315	molecular_function	iron ion sequestering activity
C	0004322	molecular_function	ferroxidase activity
C	0005506	molecular_function	iron ion binding
C	0005737	cellular_component	cytoplasm
C	0005829	cellular_component	cytosol
C	0006811	biological_process	monoatomic ion transport
C	0006826	biological_process	iron ion transport
C	0006879	biological_process	intracellular iron ion homeostasis
C	0008199	molecular_function	ferric iron binding
C	0016491	molecular_function	oxidoreductase activity
C	0020037	molecular_function	heme binding
C	0046872	molecular_function	metal ion binding
C	0070288	cellular_component	ferritin complex
C	0140315	molecular_function	iron ion sequestering activity
D	0004322	molecular_function	ferroxidase activity
D	0005506	molecular_function	iron ion binding
D	0005737	cellular_component	cytoplasm
D	0005829	cellular_component	cytosol
D	0006811	biological_process	monoatomic ion transport
D	0006826	biological_process	iron ion transport
D	0006879	biological_process	intracellular iron ion homeostasis
D	0008199	molecular_function	ferric iron binding
D	0016491	molecular_function	oxidoreductase activity
D	0020037	molecular_function	heme binding
D	0046872	molecular_function	metal ion binding
D	0070288	cellular_component	ferritin complex
D	0140315	molecular_function	iron ion sequestering activity

Functional Information from PDB Data

site_id	AC1
Number of Residues	24
Details	binding site for residue HEM A 201

Chain	Residue
A	LEU19
A	HOH421
A	HOH448
A	HOH460
A	HOH461
A	HOH463
B	LEU19
B	ILE22
B	ASN23
B	PHE26
B	TYR45
A	ILE22
B	ILE49
B	MET52
B	LYS53
B	ILE59
B	LEU71
A	ASN23
A	PHE26
A	TYR45
A	ILE49
A	MET52
A	LYS53
A	HOH387

site_id	AC2
Number of Residues	7
Details	binding site for residue MPD A 202

Chain	Residue
A	LYS2
A	GLY3
A	VAL111
A	HIS112
A	ASP113
A	HOH389
D	ARG102

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

Chain	Residue
A	ARG39
A	HIS43
A	TYR133
A	HOH416
C	LYS38
C	HOH327

site_id	AC4
Number of Residues	4
Details	binding site for residue MPD A 204

Chain	Residue
A	ARG61
A	HOH411
A	HOH492
D	GLU129

site_id	AC5
Number of Residues	5
Details	binding site for residue NA A 205

Chain	Residue
A	ASP132
A	THR136
A	HOH322
C	ASP34
C	HOH312

site_id	AC6
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	AC7
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	HOH355

site_id	AC8
Number of Residues	5
Details	binding site for residue MPD B 203

Chain	Residue
A	LYS38
A	HOH331
B	ARG39
B	HIS43
B	HOH356

site_id	AC9
Number of Residues	7
Details	binding site for residue MPD B 204

Chain	Residue
B	GLU60
B	ARG61
B	PHE64
B	GLU129
B	HOH302
B	HOH336
B	HOH489

site_id	AD1
Number of Residues	5
Details	binding site for residue NA B 205

Chain	Residue
A	ASP34
A	HOH323
B	ASP132
B	THR136
B	HOH320

site_id	AD2
Number of Residues	19
Details	binding site for residue HEM C 201

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	HOH301
C	HOH301
C	HOH302
C	HOH303
C	HOH303

site_id	AD3
Number of Residues	7
Details	binding site for residue MPD C 202

Chain	Residue
C	GLY3
C	VAL111
C	HIS112
C	ASP113
C	HOH374
A	ARG102
C	LYS2

site_id	AD4
Number of Residues	6
Details	binding site for residue MPD C 203

Chain	Residue
C	ARG39
C	HIS43
C	TYR133
C	HOH470
D	LYS38
D	HIS155

site_id	AD5
Number of Residues	5
Details	binding site for residue MPD C 204

Chain	Residue
A	GLU129
C	GLU60
C	ARG61
C	HOH304
C	HOH472

site_id	AD6
Number of Residues	6
Details	binding site for residue NA C 205

Chain	Residue
C	ASP132
C	THR136
C	HOH341
C	HOH360
D	ASP34
D	HOH474

site_id	AD7
Number of Residues	18
Details	binding site for residue HEM D 201

Chain	Residue
D	LEU19
D	ILE22
D	ASN23
D	ASN23
D	PHE26
D	PHE26
D	TYR45
D	TYR45
D	ILE49
D	ILE49
D	MET52
D	MET52
D	LYS53
D	ILE59
D	HOH301
D	HOH301
D	HOH306
D	HOH306

site_id	AD8
Number of Residues	7
Details	binding site for residue MPD D 202

Chain	Residue
C	ARG102
D	LYS2
D	GLY3
D	VAL111
D	HIS112
D	ASP113
D	HOH339

site_id	AD9
Number of Residues	8
Details	binding site for residue MPD D 203

Chain	Residue
B	LYS38
B	HIS155
B	HOH492
D	ARG39
D	HIS43
D	TYR133
D	HOH356
D	HOH436

site_id	AE1
Number of Residues	5
Details	binding site for residue MPD D 204

Chain	Residue
C	GLU129
D	GLU60
D	ARG61
D	HOH303
D	HOH370

site_id	AE2
Number of Residues	6
Details	binding site for residue NA D 205

Chain	Residue
B	ASP34
B	HOH347
D	ASP132
D	THR136
D	HOH333
D	HOH475

Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
A	MET1-LEU19

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	24
Details	BINDING: BINDING => ECO:0000269\|PubMed:20067302, ECO:0000269\|PubMed:25640193, ECO:0007744\|PDB:3IS8, ECO:0007744\|PDB:4TOH, ECO:0007744\|PDB:5D8P

Chain	Residue	Details
A	GLU18
B	GLU94
B	GLU127
B	HIS130
C	GLU18
C	GLU51
C	HIS54
C	GLU94
C	GLU127
C	HIS130
D	GLU18
A	GLU51
D	GLU51
D	HIS54
D	GLU94
D	GLU127
D	HIS130
A	HIS54
A	GLU94
A	GLU127
A	HIS130
B	GLU18
B	GLU51
B	HIS54

site_id	SWS_FT_FI2
Number of Residues	4
Details	BINDING: axial binding residue => ECO:0000269\|PubMed:20067302, ECO:0000269\|PubMed:22812654, ECO:0000269\|PubMed:25640193, ECO:0007744\|PDB:3IS8, ECO:0007744\|PDB:4E6K, ECO:0007744\|PDB:4TOH, ECO:0007744\|PDB:5D8P, ECO:0007744\|PDB:7K5E

Chain	Residue	Details
A	MET52
B	MET52
C	MET52
D	MET52

site_id	SWS_FT_FI3
Number of Residues	8
Details	BINDING: BINDING => ECO:0000269\|PubMed:20067302, ECO:0000269\|PubMed:22812654, ECO:0000269\|PubMed:25640193, ECO:0007744\|PDB:3IS7, ECO:0007744\|PDB:4E6K, ECO:0007744\|PDB:4TOH, ECO:0007744\|PDB:5D8P, ECO:0007744\|PDB:7K5E

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

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