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1SOF

Crystal structure of the azotobacter vinelandii bacterioferritin at 2.6 A 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
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
G0004322molecular_functionferroxidase activity
G0005506molecular_functioniron ion binding
G0005829cellular_componentcytosol
G0006826biological_processiron ion transport
G0006879biological_processintracellular iron ion homeostasis
G0006880biological_processintracellular sequestering of iron ion
G0008199molecular_functionferric iron binding
G0016491molecular_functionoxidoreductase activity
G0020037molecular_functionheme binding
G0046872molecular_functionmetal ion binding
H0004322molecular_functionferroxidase activity
H0005506molecular_functioniron ion binding
H0005829cellular_componentcytosol
H0006826biological_processiron ion transport
H0006879biological_processintracellular iron ion homeostasis
H0006880biological_processintracellular sequestering of iron ion
H0008199molecular_functionferric iron binding
H0016491molecular_functionoxidoreductase activity
H0020037molecular_functionheme binding
H0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE FE2 A 202
ChainResidue
AGLU18
AGLU51
AHIS54
AGLU127

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE FE2 B 202
ChainResidue
BGLU18
BGLU51
BHIS54
BGLU127

site_idAC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE FE2 C 202
ChainResidue
CGLU51
CHIS54
CILE123
CGLU127
CGLU18

site_idAC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE FE2 D 202
ChainResidue
DGLU18
DGLU51
DHIS54
DGLU127

site_idAC5
Number of Residues4
DetailsBINDING SITE FOR RESIDUE FE2 E 202
ChainResidue
EGLU18
EGLU51
EHIS54
EGLU127

site_idAC6
Number of Residues4
DetailsBINDING SITE FOR RESIDUE FE2 F 202
ChainResidue
FGLU18
FGLU51
FHIS54
FGLU127

site_idAC7
Number of Residues4
DetailsBINDING SITE FOR RESIDUE FE2 G 202
ChainResidue
GGLU18
GGLU51
GHIS54
GGLU127

site_idAC8
Number of Residues4
DetailsBINDING SITE FOR RESIDUE FE2 H 202
ChainResidue
HGLU18
HGLU51
HHIS54
HGLU127

site_idAC9
Number of Residues5
DetailsBINDING SITE FOR RESIDUE FE2 A 201
ChainResidue
AGLU51
AGLU94
AGLU127
AHIS130
AHOH421

site_idBC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE FE2 B 201
ChainResidue
BGLU51
BGLU94
BGLU127
BHOH1203
BHOH1204

site_idBC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE FE2 C 201
ChainResidue
CGLU51
CGLU94
CGLU127
CHIS130

site_idBC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE FE2 D 201
ChainResidue
DGLU51
DGLU94
DGLU127
DHIS130
DHOH512
DHOH514

site_idBC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE FE2 E 201
ChainResidue
EGLU51
EGLU94
EGLU127
EHIS130
EHOH3208

site_idBC5
Number of Residues4
DetailsBINDING SITE FOR RESIDUE FE2 F 201
ChainResidue
FGLU51
FGLU94
FGLU127
FHOH318

site_idBC6
Number of Residues5
DetailsBINDING SITE FOR RESIDUE FE2 G 201
ChainResidue
GGLU51
GGLU94
GGLU127
GHOH4213
GHOH4229

site_idBC7
Number of Residues6
DetailsBINDING SITE FOR RESIDUE FE2 H 201
ChainResidue
HGLU51
HGLU94
HGLU127
HHIS130
HHOH312
HHOH330

site_idBC8
Number of Residues4
DetailsBINDING SITE FOR RESIDUE MG D 501
ChainResidue
DGLU81
DGLU85
DHOH524
HGLU85

site_idBC9
Number of Residues4
DetailsBINDING SITE FOR RESIDUE MG G 502
ChainResidue
CGLU85
GGLU81
GGLU85
GHOH4233

site_idCC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MG A 301
ChainResidue
AASP132
AGLU135
AHOH409
AHOH411
AHOH419
AHOH423

site_idCC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE MG D 302
ChainResidue
BHOH1217
BHOH1218
BHOH1220
DASP34

site_idCC3
Number of Residues3
DetailsBINDING SITE FOR RESIDUE MG C 303
ChainResidue
CHOH2203
CHOH2229
EASP34

site_idCC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE MG D 304
ChainResidue
DHOH507
DHOH516
DHOH523
DHOH528

site_idCC5
Number of Residues3
DetailsBINDING SITE FOR RESIDUE MG B 305
ChainResidue
BHOH1201
EHOH3220
BASP34

site_idCC6
Number of Residues3
DetailsBINDING SITE FOR RESIDUE MG F 306
ChainResidue
AHOH424
BHOH1216
FHOH316

site_idCC7
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MG F 307
ChainResidue
FASP34
FHOH308
GASP132
GHOH4204
GHOH4214

site_idCC8
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MG H 308
ChainResidue
GHOH4206
GHOH4210
GHOH4216
GHOH4226
GHOH4232
HHOH322

site_idCC9
Number of Residues8
DetailsBINDING SITE FOR RESIDUE BA D 401
ChainResidue
BASN148
BGLN151
CASN148
CGLN151
DASN148
DGLN151
EASN148
EGLN151

site_idDC1
Number of Residues8
DetailsBINDING SITE FOR RESIDUE BA A 402
ChainResidue
AASN148
AGLN151
FASN148
FGLN151
GASN148
GGLN151
HASN148
HGLN151

site_idDC2
Number of Residues14
DetailsBINDING SITE FOR RESIDUE HEM B 1200
ChainResidue
AASN23
APHE26
ATYR45
AILE49
AMET52
ALYS53
AALA55
AASP56
BLEU19
BILE22
BASN23
BPHE26
BTYR45
BMET52

site_idDC3
Number of Residues11
DetailsBINDING SITE FOR RESIDUE HEM C 2200
ChainResidue
CASN23
CPHE26
CTYR45
CMET52
CLYS53
CASP56
DASN23
DPHE26
DTYR45
DMET52
DLYS53

site_idDC4
Number of Residues10
DetailsBINDING SITE FOR RESIDUE HEM E 3200
ChainResidue
EASN23
EPHE26
ETYR45
EMET52
ELYS53
EILE59
FPHE26
FTYR45
FMET52
FLYS53

site_idDC5
Number of Residues9
DetailsBINDING SITE FOR RESIDUE HEM G 4200
ChainResidue
GASN23
GPHE26
GTYR45
GMET52
GALA55
HPHE26
HTYR45
HMET52
HLYS53

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

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues48
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
GGLU18
GGLU51
GHIS54
AGLU94
GGLU94
GGLU127
GHIS130
HGLU18
HGLU51
HHIS54
HGLU94
HGLU127
HHIS130
AGLU127
AHIS130
BGLU18
BGLU51
BHIS54

site_idSWS_FT_FI2
Number of Residues8
DetailsBINDING: axial binding residue => ECO:0000255|PROSITE-ProRule:PRU00085
ChainResidueDetails
AMET52
BMET52
CMET52
DMET52
EMET52
FMET52
GMET52
HMET52

219140

PDB entries from 2024-05-01

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