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3ISF

Structure of non-mineralized Bfrb (as-isolated) from Pseudomonas aeruginosa to 2.07A Resolution

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
A0070288cellular_componentferritin complex
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
B0070288cellular_componentferritin complex
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
C0070288cellular_componentferritin complex
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
D0070288cellular_componentferritin complex
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
E0020037molecular_functionheme binding
E0046872molecular_functionmetal ion binding
E0070288cellular_componentferritin complex
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
F0020037molecular_functionheme binding
F0046872molecular_functionmetal ion binding
F0070288cellular_componentferritin complex
Functional Information from PDB Data
site_idAC1
Number of Residues8
DetailsBINDING SITE FOR RESIDUE K A 159
ChainResidue
AASN148
AASN148
AGLN151
AGLN151
DASN148
DASN148
DGLN151
DGLN151

site_idAC2
Number of Residues17
DetailsBINDING SITE FOR RESIDUE HEM B 159
ChainResidue
APHE26
ATYR45
AILE49
AMET52
ALYS53
BLEU19
BILE22
BASN23
BPHE26
BTYR45
BILE49
BMET52
BLYS53
BHOH355
BHOH360
BHOH361
AASN23

site_idAC3
Number of Residues8
DetailsBINDING SITE FOR RESIDUE K B 160
ChainResidue
BASN148
BGLN151
CASN148
CGLN151
EASN148
EGLN151
FASN148
FGLN151

site_idAC4
Number of Residues15
DetailsBINDING SITE FOR RESIDUE HEM C 159
ChainResidue
CILE22
CASN23
CPHE26
CTYR45
CILE49
CMET52
CLYS53
CHOH362
CHOH363
DASN23
DPHE26
DTYR45
DILE49
DMET52
DLYS53

site_idAC5
Number of Residues15
DetailsBINDING SITE FOR RESIDUE HEM E 159
ChainResidue
ELEU19
EILE22
EASN23
EASN23
EPHE26
EPHE26
ETYR45
ETYR45
EILE49
EILE49
EMET52
EMET52
ELYS53
EHOH171
EHOH171

site_idAC6
Number of Residues20
DetailsBINDING SITE FOR RESIDUE HEM F 159
ChainResidue
FLEU19
FILE22
FILE22
FASN23
FASN23
FPHE26
FPHE26
FTYR45
FTYR45
FILE49
FILE49
FMET52
FMET52
FLYS53
FLYS53
FALA55
FHOH189
FHOH189
FHOH359
FHOH359

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

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PDB entries from 2024-07-17

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