FhuA in complex with lipopolysaccharide and rifamycin CGP4832. Determined by X-ray diffraction at 2.9 Å resolution. Released 29 Aug 2001.
Explore 1FI1 in 3D Show helices and sheets RCSB PDB PDBe
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.
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 24-29 | 6 | |
| β-strand | 32-33 | 2 | 1 |
| β-strand | 41-42 | 2 | 1 |
| α-helix | 43-45 | 3 | |
| β-strand | 50-54 | 5 | 2 |
| α-helix | 55-61 | 7 | |
| α-helix | 66-69 | 4 | |
| β-strand | 76-77 | 2 | 3 |
| β-strand | 91-92 | 2 | 3 |
| β-strand | 95 | 1 | 3 |
| α-helix | 98-100 | 3 | |
| β-strand | 104-106 | 3 | 2 |
| β-strand | 109-110 | 2 | 2 |
| β-strand | 114 | 1 | 4 |
| β-strand | 117 | 1 | 4 |
| α-helix | 123-125 | 3 | |
| β-strand | 126-133 | 8 | 2 |
| α-helix | 137-140 | 4 | |
| β-strand | 147-153 | 7 | 2 |
| β-strand | 161-169 | 9 | 5 |
| α-helix | 170-172 | 3 | |
| β-strand | 173-183 | 11 | 5 |
| β-strand | 190-202 | 13 | 5 |
| β-strand | 209-221 | 13 | 5 |
| β-strand | 227-238 | 12 | 5 |
| β-strand | 247 | 1 | 6 |
| β-strand | 250 | 1 | 7 |
| β-strand | 254 | 1 | 7 |
| β-strand | 274-289 | 16 | 5 |
| β-strand | 294-317 | 24 | 5 |
| α-helix | 321-323 | 3 | |
| α-helix | 327-330 | 4 | |
| α-helix | 337-339 | 3 | |
| β-strand | 340-366 | 27 | 5 |
| β-strand | 371-401 | 31 | 5 |
| β-strand | 409 | 1 | 8 |
| β-strand | 412 | 1 | 8 |
| β-strand | 431-452 | 22 | 5 |
| β-strand | 457-473 | 17 | 5 |
| β-strand | 478-494 | 17 | 5 |
| β-strand | 501-512 | 12 | 5 |
| β-strand | 517 | 1 | 9 |
| β-strand | 523 | 1 | 9 |
| α-helix | 524-526 | 3 | |
| β-strand | 527-538 | 12 | 5 |
| β-strand | 545-562 | 18 | 5 |
| β-strand | 570-588 | 19 | 5 |
| β-strand | 593-608 | 16 | 5 |
| β-strand | 623-632 | 10 | 5 |
| β-strand | 641-650 | 10 | 5 |
| β-strand | 653-654 | 2 | 10 |
| β-strand | 662-663 | 2 | 10 |
| α-helix | 664-665 | 2 | |
| β-strand | 666-675 | 10 | 5 |
| α-helix | 677-680 | 4 | |
| β-strand | 686-692 | 7 | 5 |
| β-strand | 700-703 | 4 | 6 |
| β-strand | 709-711 | 3 | 6 |
| β-strand | 716-724 | 9 | 5 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Ferrichrome-iron receptor | A | protein | 707 | Escherichia coli K12 | P06971 (AlphaFold model) |
>1FI1_1 FERRICHROME-IRON RECEPTOR (chains A) ESAWGPAATIAARQSATGTKTDTPIQKVPQSISVVTAEEMALHQPKSVKEALSYTPGVSV GTRGASNTYDHLIIRGFAAEGQSQNNYLNGLKLQGNFYNDAVIDPYMLERAEIMRGPVSV LYGKSSPGGLLNMVSKRPTTEPLKEVQFKAGTDSLFQTGFDFSDSLDDDGVYSYRLTGLA RSANAQQKGSEEQRYAIAPAFTWRPDDKTNFTFLSYFQNEPETGYYGWLPKEGTVEPLPN GKRLPTDFNEGAKNNTYSRNEKMVGYSFDHEFNDTFTVRQNLRFAENKTSQNSVYGYGVC SDPANAYSKQCAALAPADKGHYLARKYVVDDEKLQNFSVDTQLQSKFATGDIDHTLLTGV DFMRMRNDINAWFGYDDSVPLLNLYNPSSHHHHHHGSSVNTDFDFNAKDPANSGPYRILN KQKQTGVYVQDQAQWDKVLVTLGGRYDWADQESLNRVAGTTDKRDDKQFTWRGGVNYLFD NGVTPYFSYSESFEPSSQVGKDGNIFAPSKGKQYEVGVKYVPEDRPIVVTGAVYNLTKTN NLMADPEGSFFSVEGGEIRARGVEIEAKAALSASVNVVGSYTYTDAEYTTDTTYKGNTPA QVPKHMASLWADYTFFDGPLSGLTLGTGGRYTGSSYGDPANSFKVGSYTVVDALVRYDLA RVGMAGSNVALHVNNLFDREYVASCFNTYGCFWGAERQVVATATFRF
| ID | Name | Formula | Copies |
|---|---|---|---|
| FTT | 3-hydroxy-tetradecanoic acid | C14 H28 O3 | 6 |
| PO4 | Phosphate ion | O4 P | 2 |
| NI | Nickel (II) ion | Ni | 1 |
| MG | Magnesium ion | Mg | 1 |
| DPO | Diphosphate | O7 P2 | 2 |
| RIF | Rifamycin cgp 4832 | C49 H65 N3 O15 | 1 |
| DDQ | Decylamine-n,n-dimethyl-N-oxide | C12 H27 N O | 1 |
Water and common crystallization additives (NA) are not listed.
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:
MolViewer shows 1FI1 directly in your browser with nothing to install. Switch between cartoon, ball-and-stick, spacefill and surface views, color by chain, secondary structure or B-factor, measure distances, angles and dihedrals, and share or embed the view.