Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

3UOF

Mycobacterium tuberculosis bacterioferritin, BfrA

Functional Information from GO Data
ChainGOidnamespacecontents
A0004322molecular_functionferroxidase activity
A0005506molecular_functioniron ion binding
A0005576cellular_componentextracellular region
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0005886cellular_componentplasma membrane
A0006826biological_processiron ion transport
A0006879biological_processintracellular iron ion homeostasis
A0006880biological_processintracellular sequestering of iron ion
A0008199molecular_functionferric iron binding
A0010039biological_processresponse to iron ion
A0016491molecular_functionoxidoreductase activity
A0020037molecular_functionheme binding
A0046872molecular_functionmetal ion binding
B0004322molecular_functionferroxidase activity
B0005506molecular_functioniron ion binding
B0005576cellular_componentextracellular region
B0005737cellular_componentcytoplasm
B0005829cellular_componentcytosol
B0005886cellular_componentplasma membrane
B0006826biological_processiron ion transport
B0006879biological_processintracellular iron ion homeostasis
B0006880biological_processintracellular sequestering of iron ion
B0008199molecular_functionferric iron binding
B0010039biological_processresponse to iron ion
B0016491molecular_functionoxidoreductase activity
B0020037molecular_functionheme binding
B0046872molecular_functionmetal ion binding
C0004322molecular_functionferroxidase activity
C0005506molecular_functioniron ion binding
C0005576cellular_componentextracellular region
C0005737cellular_componentcytoplasm
C0005829cellular_componentcytosol
C0005886cellular_componentplasma membrane
C0006826biological_processiron ion transport
C0006879biological_processintracellular iron ion homeostasis
C0006880biological_processintracellular sequestering of iron ion
C0008199molecular_functionferric iron binding
C0010039biological_processresponse to iron ion
C0016491molecular_functionoxidoreductase activity
C0020037molecular_functionheme binding
C0046872molecular_functionmetal ion binding
D0004322molecular_functionferroxidase activity
D0005506molecular_functioniron ion binding
D0005576cellular_componentextracellular region
D0005737cellular_componentcytoplasm
D0005829cellular_componentcytosol
D0005886cellular_componentplasma membrane
D0006826biological_processiron ion transport
D0006879biological_processintracellular iron ion homeostasis
D0006880biological_processintracellular sequestering of iron ion
D0008199molecular_functionferric iron binding
D0010039biological_processresponse to iron ion
D0016491molecular_functionoxidoreductase activity
D0020037molecular_functionheme binding
D0046872molecular_functionmetal ion binding
E0004322molecular_functionferroxidase activity
E0005506molecular_functioniron ion binding
E0005576cellular_componentextracellular region
E0005737cellular_componentcytoplasm
E0005829cellular_componentcytosol
E0005886cellular_componentplasma membrane
E0006826biological_processiron ion transport
E0006879biological_processintracellular iron ion homeostasis
E0006880biological_processintracellular sequestering of iron ion
E0008199molecular_functionferric iron binding
E0010039biological_processresponse to iron ion
E0016491molecular_functionoxidoreductase activity
E0020037molecular_functionheme binding
E0046872molecular_functionmetal ion binding
F0004322molecular_functionferroxidase activity
F0005506molecular_functioniron ion binding
F0005576cellular_componentextracellular region
F0005737cellular_componentcytoplasm
F0005829cellular_componentcytosol
F0005886cellular_componentplasma membrane
F0006826biological_processiron ion transport
F0006879biological_processintracellular iron ion homeostasis
F0006880biological_processintracellular sequestering of iron ion
F0008199molecular_functionferric iron binding
F0010039biological_processresponse to iron ion
F0016491molecular_functionoxidoreductase activity
F0020037molecular_functionheme binding
F0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE FE A 201
ChainResidue
AGLU47
AGLU51
AGLU94
AGLU127
AHIS130

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE FE A 202
ChainResidue
AGLU18
AGLU51
AHIS54
AGLU127

site_idAC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE TRS A 203
ChainResidue
ALYS122
BLYS122
BTRS304
BHOH421
DLYS122

site_idAC4
Number of Residues12
DetailsBINDING SITE FOR RESIDUE HEM B 301
ChainResidue
APHE26
AARG45
APHE49
AMET52
AGLU56
BASN23
BPHE26
BPHE49
BMET52
BARG53
BGLU56
BTYR71

site_idAC5
Number of Residues4
DetailsBINDING SITE FOR RESIDUE FE B 302
ChainResidue
BGLU18
BGLU51
BHIS54
BGLU127

site_idAC6
Number of Residues5
DetailsBINDING SITE FOR RESIDUE FE B 303
ChainResidue
BGLU47
BGLU51
BGLU94
BGLU127
BHIS130

site_idAC7
Number of Residues6
DetailsBINDING SITE FOR RESIDUE TRS B 304
ChainResidue
AVAL118
AGLU121
ATRS203
BVAL118
BHOH421
DVAL118

site_idAC8
Number of Residues4
DetailsBINDING SITE FOR RESIDUE FE C 201
ChainResidue
CGLU18
CGLU51
CHIS54
CGLU127

site_idAC9
Number of Residues5
DetailsBINDING SITE FOR RESIDUE FE C 202
ChainResidue
CGLU47
CGLU51
CGLU94
CGLU127
CHIS130

site_idBC1
Number of Residues13
DetailsBINDING SITE FOR RESIDUE HEM D 201
ChainResidue
CLEU19
CILE22
CPHE26
CPHE49
CMET52
CARG53
CGLU56
DILE22
DASN23
DPHE26
DPHE49
DMET52
DARG53

site_idBC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE FE D 202
ChainResidue
DGLU18
DGLU51
DHIS54
DGLU127
DFE203

site_idBC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE FE D 203
ChainResidue
DGLU51
DGLU94
DGLU127
DFE202

site_idBC4
Number of Residues15
DetailsBINDING SITE FOR RESIDUE HEM E 301
ChainResidue
EILE22
EASN23
EPHE26
EARG45
EPHE49
EMET52
EARG53
FLEU19
FILE22
FPHE26
FPHE49
FMET52
FARG53
FALA55
FGLU56

site_idBC5
Number of Residues3
DetailsBINDING SITE FOR RESIDUE FE E 302
ChainResidue
EGLU51
EGLU94
EGLU127

site_idBC6
Number of Residues4
DetailsBINDING SITE FOR RESIDUE FE E 303
ChainResidue
EGLU18
EHIS54
EILE123
EGLU127

site_idBC7
Number of Residues5
DetailsBINDING SITE FOR RESIDUE FE F 201
ChainResidue
FTYR25
FGLU51
FGLU94
FGLU127
FHIS130

site_idBC8
Number of Residues4
DetailsBINDING SITE FOR RESIDUE FE F 202
ChainResidue
FGLU18
FGLU51
FHIS54
FGLU127

site_idBC9
Number of Residues6
DetailsBINDING SITE FOR RESIDUE TRS F 203
ChainResidue
CLYS122
EVAL118
FVAL118
FLYS122
FHOH309
FHOH310

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues36
DetailsBINDING:
ChainResidueDetails
AGLU18
BGLU94
BGLU127
BHIS130
CGLU18
CGLU51
CHIS54
CGLU94
CGLU127
CHIS130
DGLU18
AGLU51
DGLU51
DHIS54
DGLU94
DGLU127
DHIS130
EGLU18
EGLU51
EHIS54
EGLU94
EGLU127
AHIS54
EHIS130
FGLU18
FGLU51
FHIS54
FGLU94
FGLU127
FHIS130
AGLU94
AGLU127
AHIS130
BGLU18
BGLU51
BHIS54

site_idSWS_FT_FI2
Number of Residues6
DetailsBINDING: axial binding residue => ECO:0000255|PROSITE-ProRule:PRU00085
ChainResidueDetails
AMET52
BMET52
CMET52
DMET52
EMET52
FMET52

222926

PDB entries from 2024-07-24

PDB statisticsPDBj update infoContact PDBjnumon