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4TOG

1.80A resolution structure of BfrB (C89S, K96C) crystal form 2 from Pseudomonas aeruginosa

Functional Information from GO Data
ChainGOidnamespacecontents
A0004322molecular_functionferroxidase activity
A0005506molecular_functioniron ion binding
A0005829cellular_componentcytosol
A0006826biological_processiron ion transport
A0006879biological_processintracellular iron ion homeostasis
A0006880biological_processintracellular sequestering of iron ion
A0008199molecular_functionferric iron binding
A0020037molecular_functionheme binding
A0046872molecular_functionmetal ion binding
B0004322molecular_functionferroxidase activity
B0005506molecular_functioniron ion binding
B0005829cellular_componentcytosol
B0006826biological_processiron ion transport
B0006879biological_processintracellular iron ion homeostasis
B0006880biological_processintracellular sequestering of iron ion
B0008199molecular_functionferric iron binding
B0020037molecular_functionheme binding
B0046872molecular_functionmetal ion binding
C0004322molecular_functionferroxidase activity
C0005506molecular_functioniron ion binding
C0005829cellular_componentcytosol
C0006826biological_processiron ion transport
C0006879biological_processintracellular iron ion homeostasis
C0006880biological_processintracellular sequestering of iron ion
C0008199molecular_functionferric iron binding
C0020037molecular_functionheme binding
C0046872molecular_functionmetal ion binding
D0004322molecular_functionferroxidase activity
D0005506molecular_functioniron ion binding
D0005829cellular_componentcytosol
D0006826biological_processiron ion transport
D0006879biological_processintracellular iron ion homeostasis
D0006880biological_processintracellular sequestering of iron ion
D0008199molecular_functionferric iron binding
D0020037molecular_functionheme binding
D0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues24
Detailsbinding site for residue HEM A 201
ChainResidue
ALEU19
AHOH375
AHOH412
AHOH413
AHOH422
AHOH457
AHOH461
BLEU19
BILE22
BASN23
BPHE26
AILE22
BTYR45
BILE49
BMET52
BLYS53
BLEU71
AASN23
APHE26
ATYR45
AILE49
AMET52
ALYS53
AHOH364

site_idAC2
Number of Residues6
Detailsbinding site for residue MPD A 202
ChainResidue
ALYS2
AGLY3
AVAL111
AASP113
AHOH377
DARG102

site_idAC3
Number of Residues2
Detailsbinding site for residue MPD A 203
ChainResidue
AARG61
AHOH383

site_idAC4
Number of Residues4
Detailsbinding site for residue NA A 204
ChainResidue
ATHR136
AHOH335
AHOH343
CASP34

site_idAC5
Number of Residues8
Detailsbinding site for residue K B 201
ChainResidue
AASN148
AGLN151
BASN148
BGLN151
CASN148
CGLN151
DASN148
DGLN151

site_idAC6
Number of Residues6
Detailsbinding site for residue MPD B 202
ChainResidue
BLYS2
BGLY3
BARG102
BVAL111
BASP113
BHOH366

site_idAC7
Number of Residues4
Detailsbinding site for residue MPD B 203
ChainResidue
BGLU60
BARG61
BHOH306
BHOH354

site_idAC8
Number of Residues5
Detailsbinding site for residue NA B 204
ChainResidue
AASP34
AHOH333
BASP132
BTHR136
BHOH311

site_idAC9
Number of Residues9
Detailsbinding site for residue SO4 B 205
ChainResidue
BARG117
BARG117
BASP118
BASP118
BASP118
BLYS121
BLYS121
BLYS121
BHOH314

site_idAD1
Number of Residues18
Detailsbinding site for residue HEM C 201
ChainResidue
CLEU19
CILE22
CASN23
CASN23
CPHE26
CPHE26
CTYR45
CTYR45
CILE49
CILE49
CMET52
CMET52
CLYS53
CLYS53
CHOH303
CHOH303
CHOH304
CHOH304

site_idAD2
Number of Residues3
Detailsbinding site for residue MPD C 202
ChainResidue
CGLU60
CARG61
CHOH335

site_idAD3
Number of Residues5
Detailsbinding site for residue NA C 203
ChainResidue
CASP132
CTHR136
CHOH317
DASP34
DHOH457

site_idAD4
Number of Residues18
Detailsbinding site for residue HEM D 201
ChainResidue
DPHE26
DTYR45
DTYR45
DILE49
DMET52
DMET52
DLYS53
DLYS53
DLEU71
DHOH301
DHOH301
DHOH307
DHOH307
DLEU19
DILE22
DASN23
DASN23
DPHE26

site_idAD5
Number of Residues5
Detailsbinding site for residue MPD D 202
ChainResidue
DLYS2
DGLY3
DVAL111
DASP113
DHOH342

site_idAD6
Number of Residues3
Detailsbinding site for residue MPD D 203
ChainResidue
DARG61
DHOH310
DHOH416

site_idAD7
Number of Residues5
Detailsbinding site for residue NA D 204
ChainResidue
BASP34
BHOH454
DASP132
DTHR136
DHOH455

site_idAD8
Number of Residues12
Detailsbinding site for residue SO4 D 205
ChainResidue
AARG117
AASP118
ALYS121
CARG117
CASP118
CLYS121
DARG117
DASP118
DLYS121
DHOH317
DHOH325
DHOH354

Functional Information from PROSITE/UniProt
site_idPS00549
Number of Residues19
DetailsBACTERIOFERRITIN Bacterioferritin signature. MkGdkkVIqhLnkiLgneL
ChainResidueDetails
AMET1-LEU19

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PDB entries from 2024-06-12

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