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1BY3

FHUA FROM E. COLI

Functional Information from GO Data
ChainGOidnamespacecontents
A0005506molecular_functioniron ion binding
A0005515molecular_functionprotein binding
A0006811biological_processmonoatomic ion transport
A0006826biological_processiron ion transport
A0006879biological_processintracellular iron ion homeostasis
A0009279cellular_componentcell outer membrane
A0015343molecular_functionsiderophore-iron transmembrane transporter activity
A0015344molecular_functionsiderophore uptake transmembrane transporter activity
A0015643molecular_functiontoxic substance binding
A0015891biological_processsiderophore transport
A0016020cellular_componentmembrane
A0019904molecular_functionprotein domain specific binding
A0033214biological_processsiderophore-iron import into cell
A0038023molecular_functionsignaling receptor activity
A0044718biological_processsiderophore transmembrane transport
A0046790molecular_functionvirion binding
A1902495cellular_componenttransmembrane transporter complex
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE OES A 715
ChainResidue
ATHR176
ASER200
APHE290
AASN291
APHE294

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE OES A 716
ChainResidue
ATYR284
AGLN298
AVAL676
AALA710

site_idAC3
Number of Residues3
DetailsBINDING SITE FOR RESIDUE OES A 717
ChainResidue
APHE302
APHE355
AVAL669

site_idAC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE OES A 718
ChainResidue
ATYR116
ATRP246
AGLN309
ASER311
ATYR313

site_idAC5
Number of Residues1
DetailsBINDING SITE FOR RESIDUE OES A 719
ChainResidue
ATYR213

site_idAC6
Number of Residues3
DetailsBINDING SITE FOR RESIDUE OES A 720
ChainResidue
AALA214
AILE215
APHE235

site_idAC7
Number of Residues6
DetailsBINDING SITE FOR RESIDUE OES A 721
ChainResidue
AVAL164
ATRP455
AASP457
AASP472
APHE714
AHOH1072

Functional Information from PROSITE/UniProt
site_idPS01156
Number of Residues18
DetailsTONB_DEPENDENT_REC_2 TonB-dependent receptor (TBDR) proteins signature 2. GcfwGaERqVvATAtFrF
ChainResidueDetails
AGLY697-PHE714

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues204
DetailsTOPO_DOM: Periplasmic
ChainResidueDetails
AALA1-GLU159
APHE622-SER628
ALEU666-ALA672
APHE714
ASER183-VAL189
APRO223-LYS226
AGLU289-THR293
ALYS364-ASP371
AGLN441-LYS444
ALEU485-GLY489
AVAL528-ARG532
ALEU578-ALA580

site_idSWS_FT_FI2
Number of Residues177
DetailsTRANSMEM: Beta stranded
ChainResidueDetails
APRO160-ALA168
ATHR432-ALA440
AVAL445-TYR453
APHE476-TYR484
AVAL490-GLU498
ALYS519-TYR527
APRO533-TYR541
AGLY569-PRO577
ASER581-THR589
AMET613-THR621
AGLY629-ARG637
APHE174-ASP182
AVAL657-ASP665
AGLY673-ASN681
AGLN705-ARG713
ATYR190-ALA198
ATYR213-ARG222
ATHR227-PHE235
ALYS280-HIS288
APHE294-PHE302
APHE355-SER363
AHIS372-PHE380

site_idSWS_FT_FI3
Number of Residues289
DetailsTOPO_DOM: Extracellular
ChainResidueDetails
AGLY169-LEU173
ATYR638-THR656
AASN682-ARG704
AARG199-ARG212
AGLN236-GLU279
AALA303-ASN354
AMET381-GLN431
AASP454-GLN475
ASER499-GLY518
AASN542-ARG568
ATYR590-HIS612

site_idSWS_FT_FI4
Number of Residues5
DetailsBINDING: BINDING => ECO:0000305|PubMed:10850805, ECO:0000305|PubMed:9856937, ECO:0000305|PubMed:9865695
ChainResidueDetails
AARG81
AGLN100
APHE115
ATYR244
ATYR313

site_idSWS_FT_FI5
Number of Residues2
DetailsBINDING: BINDING => ECO:0000305|PubMed:9856937
ChainResidueDetails
APHE391
AALA702

site_idSWS_FT_FI6
Number of Residues1
DetailsSITE: Interaction with phage T5 RBP-pb5 => ECO:0000269|PubMed:36779755
ChainResidueDetails
APRO533

238268

PDB entries from 2025-07-02

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