2FCP: Protein

Ferric hydroxamate uptake receptor (FHUA) from e.coli. Determined by X-ray diffraction at 2.5 Å resolution. Released 13 Jan 1999.

Method
X-ray diffraction
Resolution
2.5 Å
Organism
Escherichia coli
Chains
1
Atoms
5,833
Mol. weight
83.37 kDa
Ligands
EA2, LIM, AAE, LIL
Released
13 Jan 1999

Explore 2FCP in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

2FCP contains 15 α-helices and 43 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: 15 helices, 43 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-strand340-366275
β-strand371-401315
α-helix407-4104
β-strand429-450225
β-strand454-471185
β-strand476-493185
β-strand499-510125
β-strand51518
β-strand52118
α-helix522-5243
β-strand525-536125
β-strand543-560185
β-strand568-586195
β-strand591-606165
α-helix613-6153
β-strand621-631115
β-strand639-648105
β-strand651-65229
β-strand660-66129
α-helix662-6632
β-strand664-673105
β-strand684-69075
β-strand698-70366
β-strand706-70946
β-strand714-72295

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Protein (ferric hydroxamate uptake receptor)Aprotein723Escherichia coliP06971 (AlphaFold model)
Sequence of entity 1 (A), FASTA
>2FCP_1 PROTEIN (FERRIC HYDROXAMATE UPTAKE RECEPTOR) (chains A)
AVEPKEDTITVTAAPAPQESAWGPAATIAARQSATGTKTDTPIQKVPQSISVVTAEEMAL
HQPKSVKEALSYTPGVSVGTRGASNTYDHLIIRGFAAEGQSQNNYLNGLKLQGNFYNDAV
IDPYMLERAEIMRGPVSVLYGKSSPGGLLNMVSKRPTTEPLKEVQFKAGTDSLFQTGFDF
SDSLDDDGVYSYRLTGLARSANAQQKGSEEQRYAIAPAFTWRPDDKTNFTFLSYFQNEPE
TGYYGWLPKEGTVEPLPNGKRLPTDFNEGAKNNTYSRNEKMVGYSFDHEFNDTFTVRQNL
RFAENKTSQNSVYGYGVCSDPANAYSKQCAALAPADKGHYLARKYVVDDEKLQNFSVDTQ
LQSKFATGDIDHTLLTGVDFMRMRNDINAWFGYDDSVPLLNLYNPSHHHHHHGSVNTDFD
FNAKDPANSGPYRILNKQKQTGVYVQDQAQWDKVLVTLGGRYDWADQESLNRVAGTTDKR
DDKQFTWRGGVNYLFDNGVTPYFSYSESFEPSSQVGKDGNIFAPSKGKQYEVGVKYVPED
RPIVVTGAVYNLTKTNNLMADPEGSFFSVEGGEIRARGVEIEAKAALSASVNVVGSYTYT
DAEYTTDTTYKGNTPAQVPKHMASLWADYTFFDGPLSGLTLGTGGRYTGSSYGDPANSFK
VGSYTVVDALVRYDLARVGMAGSNVALHVNNLFDREYVASCFNTYGCFWGAERQVVATAT
FRF

Ligands and cofactors

IDNameFormulaCopies
EA2AminoethanolpyrophosphateC2 H9 N O7 P21
LIM3-oxo-pentadecanoic acidC15 H28 O31
AAEAcetoacetic acidC4 H6 O31
LIL2-tridecanoyloxy-pentadecanoic acidC28 H54 O42
NINickel (II) ionNi2

Primary citation

Siderophore-mediated iron transport: crystal structure of FhuA with bound lipopolysaccharide. Ferguson, A.D., Hofmann, E., Coulton, J.W. et al. Science (1998) 282:2215-2220. DOI 10.1126/science.282.5397.2215 · 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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