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1JGC

The 2.6 A Structure Resolution of Rhodobacter capsulatus Bacterioferritin with Metal-free Dinuclear Site and Heme Iron in a Crystallographic Special Position

Functional Information from GO Data
ChainGOidnamespacecontents
A0004322molecular_functionferroxidase activity
A0005506molecular_functioniron ion binding
A0005829cellular_componentcytosol
A0006826biological_processiron ion transport
A0006879biological_processintracellular iron ion homeostasis
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
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
C0008199molecular_functionferric iron binding
C0016491molecular_functionoxidoreductase activity
C0020037molecular_functionheme binding
C0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues10
DetailsBINDING SITE FOR RESIDUE HEM B 200
ChainResidue
ALEU19
BMET52
ATRP26
AARG45
AMET52
AALA55
AHEM201
BLEU19
BTRP26
BARG45

site_idAC2
Number of Residues9
DetailsBINDING SITE FOR RESIDUE HEM A 201
ChainResidue
ALEU19
ATRP26
AARG45
AMET52
BSER23
BTRP26
BARG45
BMET52
BHEM200

site_idAC3
Number of Residues10
DetailsBINDING SITE FOR RESIDUE HEM C 202
ChainResidue
CLEU19
CILE22
CSER23
CTRP26
CTRP26
CARG45
CARG45
CILE49
CMET52
CMET52

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

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues432
DetailsDomain: {"description":"Ferritin-like diiron","evidences":[{"source":"PROSITE-ProRule","id":"PRU00085","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues18
DetailsBinding site: {}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues3
DetailsBinding site: {"description":"axial binding residue"}
ChainResidueDetails

249697

PDB entries from 2026-02-25

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