1FI1: FhuA

FhuA in complex with lipopolysaccharide and rifamycin CGP4832. Determined by X-ray diffraction at 2.9 Å resolution. Released 29 Aug 2001.

Method
X-ray diffraction
Resolution
2.9 Å
Organism
Escherichia coli K12
Chains
1
Atoms
6,030
Mol. weight
83.47 kDa
Ligands
FTT, PO4, NI, MG
Released
29 Aug 2001

Explore 1FI1 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

1FI1 contains 14 α-helices and 45 β-strands across 1 chain. Residue ranges use author residue numbering, as in the PDB file, from PDBe. To see them in 3D, choose the Cartoon representation with Secondary structure coloring: helices, sheets and coils get different colors.

Chain A: 14 helices, 45 β-strands

ElementResiduesLengthSheet
α-helix24-296
β-strand32-3321
β-strand41-4221
α-helix43-453
β-strand50-5452
α-helix55-617
α-helix66-694
β-strand76-7723
β-strand91-9223
β-strand9513
α-helix98-1003
β-strand104-10632
β-strand109-11022
β-strand11414
β-strand11714
α-helix123-1253
β-strand126-13382
α-helix137-1404
β-strand147-15372
β-strand161-16995
α-helix170-1723
β-strand173-183115
β-strand190-202135
β-strand209-221135
β-strand227-238125
β-strand24716
β-strand25017
β-strand25417
β-strand274-289165
β-strand294-317245
α-helix321-3233
α-helix327-3304
α-helix337-3393
β-strand340-366275
β-strand371-401315
β-strand40918
β-strand41218
β-strand431-452225
β-strand457-473175
β-strand478-494175
β-strand501-512125
β-strand51719
β-strand52319
α-helix524-5263
β-strand527-538125
β-strand545-562185
β-strand570-588195
β-strand593-608165
β-strand623-632105
β-strand641-650105
β-strand653-654210
β-strand662-663210
α-helix664-6652
β-strand666-675105
α-helix677-6804
β-strand686-69275
β-strand700-70346
β-strand709-71136
β-strand716-72495

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Ferrichrome-iron receptorAprotein707Escherichia coli K12P06971 (AlphaFold model)
Sequence of entity 1 (A), FASTA
>1FI1_1 FERRICHROME-IRON RECEPTOR (chains A)
ESAWGPAATIAARQSATGTKTDTPIQKVPQSISVVTAEEMALHQPKSVKEALSYTPGVSV
GTRGASNTYDHLIIRGFAAEGQSQNNYLNGLKLQGNFYNDAVIDPYMLERAEIMRGPVSV
LYGKSSPGGLLNMVSKRPTTEPLKEVQFKAGTDSLFQTGFDFSDSLDDDGVYSYRLTGLA
RSANAQQKGSEEQRYAIAPAFTWRPDDKTNFTFLSYFQNEPETGYYGWLPKEGTVEPLPN
GKRLPTDFNEGAKNNTYSRNEKMVGYSFDHEFNDTFTVRQNLRFAENKTSQNSVYGYGVC
SDPANAYSKQCAALAPADKGHYLARKYVVDDEKLQNFSVDTQLQSKFATGDIDHTLLTGV
DFMRMRNDINAWFGYDDSVPLLNLYNPSSHHHHHHGSSVNTDFDFNAKDPANSGPYRILN
KQKQTGVYVQDQAQWDKVLVTLGGRYDWADQESLNRVAGTTDKRDDKQFTWRGGVNYLFD
NGVTPYFSYSESFEPSSQVGKDGNIFAPSKGKQYEVGVKYVPEDRPIVVTGAVYNLTKTN
NLMADPEGSFFSVEGGEIRARGVEIEAKAALSASVNVVGSYTYTDAEYTTDTTYKGNTPA
QVPKHMASLWADYTFFDGPLSGLTLGTGGRYTGSSYGDPANSFKVGSYTVVDALVRYDLA
RVGMAGSNVALHVNNLFDREYVASCFNTYGCFWGAERQVVATATFRF

Ligands and cofactors

IDNameFormulaCopies
FTT3-hydroxy-tetradecanoic acidC14 H28 O36
PO4Phosphate ionO4 P2
NINickel (II) ionNi1
MGMagnesium ionMg1
DPODiphosphateO7 P22
RIFRifamycin cgp 4832C49 H65 N3 O151
DDQDecylamine-n,n-dimethyl-N-oxideC12 H27 N O1

Water and common crystallization additives (NA) are not listed.

Primary citation

Active transport of an antibiotic rifamycin derivative by the outer-membrane protein FhuA. Ferguson, A.D., Kodding, J., Walker, G. et al. Structure (2001) 9:707-716. DOI 10.1016/S0969-2126(01)00631-1 · PubMed

Other PDB entries of the same protein (UniProt P06971 (AlphaFold model), which also has an AlphaFold model), best resolution first:

Browse structure collections

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