1QFG: E. Coli ferric hydroxamate receptor

E. Coli ferric hydroxamate receptor (FHUA). Determined by X-ray diffraction at 2.5 Å resolution. Released 26 Jul 2000.

Method
X-ray diffraction
Resolution
2.5 Å
Organism
Escherichia coli
Chains
1
Atoms
6,077
Mol. weight
85.03 kDa
Ligands
DPO, DDQ, MYR, DAO
Released
26 Jul 2000

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

Secondary structure: helices and β-sheets

1QFG contains 16 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: 16 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-strand174-183105
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-strand340-367285
β-strand370-401325
α-helix408-4136
β-strand431-453235
β-strand456-473185
β-strand478-495185
β-strand49718
β-strand50118
β-strand502-512115
β-strand51719
β-strand52319
α-helix524-5263
β-strand527-538125
β-strand545-562185
β-strand570-590215
β-strand593-608165
α-helix615-6173
β-strand623-633115
β-strand641-650105
β-strand653-654210
β-strand662-663210
α-helix664-6652
β-strand666-675105
α-helix677-6804
β-strand686-69275
β-strand700-70566
β-strand708-71146
β-strand716-72495

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Protein (ferric hydroxamate uptake receptor)Aprotein725Escherichia coliP06971 (AlphaFold model)
Sequence of entity 1 (A), FASTA
>1QFG_1 PROTEIN (FERRIC HYDROXAMATE UPTAKE RECEPTOR) (chains A)
AVEPKEDTITVTAAPAPQESAWGPAATIAARQSATGTKTDTPIQKVPQSISVVTAEEMAL
HQPKSVKEALSYTPGVSVGTRGASNTYDHLIIRGFAAEGQSQNNYLNGLKLQGNFYNDAV
IDPYMLERAEIMRGPVSVLYGKSSPGGLLNMVSKRPTTEPLKEVQFKAGTDSLFQTGFDF
SDSLDDDGVYSYRLTGLARSANAQQKGSEEQRYAIAPAFTWRPDDKTNFTFLSYFQNEPE
TGYYGWLPKEGTVEPLPNGKRLPTDFNEGAKNNTYSRNEKMVGYSFDHEFNDTFTVRQNL
RFAENKTSQNSVYGYGVCSDPANAYSKQCAALAPADKGHYLARKYVVDDEKLQNFSVDTQ
LQSKFATGDIDHTLLTGVDFMRMRNDINAWFGYDDSVPLLNLYNPSSHHHHHHGSSVNTD
FDFNAKDPANSGPYRILNKQKQTGVYVQDQAQWDKVLVTLGGRYDWADQESLNRVAGTTD
KRDDKQFTWRGGVNYLFDNGVTPYFSYSESFEPSSQVGKDGNIFAPSKGKQYEVGVKYVP
EDRPIVVTGAVYNLTKTNNLMADPEGSFFSVEGGEIRARGVEIEAKAALSASVNVVGSYT
YTDAEYTTDTTYKGNTPAQVPKHMASLWADYTFFDGPLSGLTLGTGGRYTGSSYGDPANS
FKVGSYTVVDALVRYDLARVGMAGSNVALHVNNLFDREYVASCFNTYGCFWGAERQVVAT
ATFRF

Ligands and cofactors

IDNameFormulaCopies
DPODiphosphateO7 P22
DDQDecylamine-n,n-dimethyl-N-oxideC12 H27 N O3
MYRMyristic acidC14 H28 O21
DAOLauric acidC12 H24 O21
FTT3-hydroxy-tetradecanoic acidC14 H28 O34
PO4Phosphate ionO4 P2
NINickel (II) ionNi1

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

Primary citation

A conserved structural motif for lipopolysaccharide recognition by procaryotic and eucaryotic proteins. Ferguson, A.D., Welte, W., Hofmann, E. et al. Structure (2000) 8:585-592. DOI 10.1016/S0969-2126(00)00143-X · 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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