3SKP: Serotransferrin

The structure of apo-human transferrin C-lobe with bound sulfate ions. Determined by X-ray diffraction at 1.7 Å resolution. Released 15 Feb 2012.

Method: X-ray diffraction
Resolution: 1.7 Å
Organism: Homo sapiens
Chains: 1
Atoms: 3,002
Mol. weight: 38.78 kDa
Released: 15 Feb 2012

Explore 3SKP in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

3SKP contains 22 α-helices and 14 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: 22 helices, 14 β-strands

Element	Residues	Length	Sheet
α-helix	340	1
β-strand	342-346	5	1
α-helix	349-361	13
β-strand	366-370	5	1
α-helix	374-383	10
β-strand	388	1	1
β-strand	389-391	3	2
α-helix	393-401	9
β-strand	405-411	7	2
α-helix	418-420	3
β-strand	426-433	8	3
α-helix	441-443	3
β-strand	448-451	4	3
α-helix	457-461	5
α-helix	462-466	5
α-helix	468-470	3
α-helix	476-478	3
β-strand	482-484	3	3
α-helix	493-495	3
α-helix	502-504	3
α-helix	516-526	11
β-strand	530-534	5	3
α-helix	537-540	4
α-helix	556-558	3
β-strand	559-562	4	3
β-strand	568-570	3	3
α-helix	571-576	6
β-strand	580-582	3	3
α-helix	583-585	3
β-strand	586-589	4	2
α-helix	591-593	3
α-helix	594-608	15
β-strand	637-640	4	2
α-helix	647-650	4
α-helix	653-665	13
α-helix	669-675	7

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Serotransferrin	A	protein	342	Homo sapiens	P02787 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>3SKP_1 Serotransferrin (chains A)
GCKPVKWCALSHHERLKCDEWSVNSVGKIECVSAETTEDCIAKIMNGEADAMSLDGGFVY
IAGKCGLVPVLAENYNKSDNCEDTPEAGYFAVAVVKKSASDLTWDNLKGKKSCHTAVGRT
AGWNIPMGLLYNKINHCRFDEFFSEGCAPGSKKDSSLCKLCMGSGLNLCEPNNKEGYYGY
TGAFRCLVEKGDVAFVKHQTVPQNTGGKNPDPWAKNLNEKDYELLCLDGTRKPVEEYANC
HLARAPNHAVVTRKDKEACVHKILRQQQHLFGSNVTDCSGNFCLFRSETKDLLFRDDTVC
LAKLHDRNTYEKYLGEEYVKAVGNLRKCSTSSLLEACTFRRP

Primary citation

Structural basis for iron piracy by pathogenic Neisseria. Noinaj, N., Easley, N.C., Oke, M. et al. Nature (2012) 483:53-58. DOI 10.1038/nature10823 · PubMed

Other PDB entries of the same protein (UniProt P02787 (AlphaFold model), which also has an AlphaFold model), best resolution first:

1RYO 1.2 Å, Human serum transferrin, N-lobe bound with oxalate
1A8E 1.6 Å, Human serum transferrin, recombinant N-terminal lobe
1A8F 1.8 Å, Human serum transferrin, recombinant N-terminal lobe
1D3K 1.8 Å, Human serum transferrin
1FQE 1.8 Å, Crystal structures of mutant (K206A) that abolish the dilysine interaction in the N-lobe…
3FGS 1.8 Å, Crystal structure of G65R/K206E double mutant of the N-lobe human transferrin
1JQF 1.85 Å, Human Transferrin N-Lobe Mutant H249Q
1OQG 1.9 Å, Crystal structure of the D63E mutant of the N-lobe human transferrin
9RTB 1.93 Å, Crystal structure of the adduct formed upon reaction of [V(IV)O(acetylacetonate)2] with…
1D4N 2.0 Å, Human serum transferrin
1N84 2.05 Å, Human serum transferrin, N-lobe
1FQF 2.1 Å, Crystal structures of mutant (K296A) that abolish the dilysine interaction in the N-lobe…

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