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5XX9

Crystal structure of Bacterioferritin

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
A0016491molecular_functionoxidoreductase activity
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
B0016491molecular_functionoxidoreductase activity
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
C0016491molecular_functionoxidoreductase activity
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
D0016491molecular_functionoxidoreductase activity
D0020037molecular_functionheme binding
D0046872molecular_functionmetal ion binding
E0004322molecular_functionferroxidase activity
E0005506molecular_functioniron ion binding
E0005829cellular_componentcytosol
E0006826biological_processiron ion transport
E0006879biological_processintracellular iron ion homeostasis
E0006880biological_processintracellular sequestering of iron ion
E0008199molecular_functionferric iron binding
E0016491molecular_functionoxidoreductase activity
E0020037molecular_functionheme binding
E0046872molecular_functionmetal ion binding
F0004322molecular_functionferroxidase activity
F0005506molecular_functioniron ion binding
F0005829cellular_componentcytosol
F0006826biological_processiron ion transport
F0006879biological_processintracellular iron ion homeostasis
F0006880biological_processintracellular sequestering of iron ion
F0008199molecular_functionferric iron binding
F0016491molecular_functionoxidoreductase activity
F0020037molecular_functionheme binding
F0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues4
Detailsbinding site for residue FE2 A 201
ChainResidue
AGLU18
AGLU51
AHIS54
AGLU127

site_idAC2
Number of Residues1
Detailsbinding site for residue FE2 A 202
ChainResidue
AHOH411

site_idAC3
Number of Residues4
Detailsbinding site for residue FE2 B 200
ChainResidue
BGLU18
BGLU51
BHIS54
BGLU127

site_idAC4
Number of Residues4
Detailsbinding site for residue FE2 C 201
ChainResidue
CGLU18
CGLU51
CHIS54
CGLU127

site_idAC5
Number of Residues2
Detailsbinding site for residue FE2 C 202
ChainResidue
DFE2202
DHOH405

site_idAC6
Number of Residues4
Detailsbinding site for residue FE2 D 201
ChainResidue
DGLU18
DGLU51
DHIS54
DGLU127

site_idAC7
Number of Residues1
Detailsbinding site for residue FE2 D 202
ChainResidue
CFE2202

site_idAC8
Number of Residues4
Detailsbinding site for residue FE2 E 201
ChainResidue
EGLU18
EGLU51
EHIS54
EGLU127

site_idAC9
Number of Residues1
Detailsbinding site for residue FE2 E 202
ChainResidue
FHOH399

site_idAD1
Number of Residues2
Detailsbinding site for residue FE2 E 203
ChainResidue
EASN23
EHOH489

site_idAD2
Number of Residues4
Detailsbinding site for residue FE2 F 200
ChainResidue
FGLU18
FGLU51
FHIS54
FGLU127

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

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues36
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00085
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

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PDB entries from 2024-07-31

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