1A8E: Serum transferrin

Human serum transferrin, recombinant N-terminal lobe. Determined by X-ray diffraction at 1.6 Å resolution. Released 17 Jun 1998.

Method
X-ray diffraction
Resolution
1.6 Å
Organism
Homo sapiens
Chains
1
Atoms
2,714
Mol. weight
36.52 kDa
Ligands
CO3, FE
Released
17 Jun 1998

Explore 1A8E in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

1A8E contains 20 α-helices and 16 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: 20 helices, 16 β-strands

ElementResiduesLengthSheet
β-strand4-1181
α-helix12-2918
β-strand35-4281
α-helix45-539
β-strand5911
β-strand60-6232
α-helix64-718
β-strand77-8482
β-strand8513
β-strand9213
β-strand94-10294
α-helix109-1113
β-strand117-11934
α-helix125-1295
α-helix130-1356
α-helix136-1383
α-helix1401
α-helix1421
α-helix146-1538
β-strand157-15824
α-helix168-1714
α-helix187-19610
β-strand202-20654
α-helix209-2135
α-helix217-2204
β-strand223-22754
β-strand231-23444
α-helix235-2406
β-strand244-24744
α-helix248-2492
β-strand250-25452
α-helix260-27415
β-strand301-30442
α-helix305-3062
α-helix311-3155
α-helix317-32711

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Serum transferrinAprotein329Homo sapiensP02787 (AlphaFold model)
Sequence of entity 1 (A), FASTA
>1A8E_1 SERUM TRANSFERRIN (chains A)
DKTVRWCAVSEHEATKCQSFRDHMKSVIPSDGPSVACVKKASYLDCIRAIAANEADAVTL
DAGLVYDAYLAPNNLKPVVAEFYGSKEDPQTFYYAVAVVKKDSGFQMNQLRGKKSCHTGL
GRSAGWNIPIGLLYCDLPEPRKPLEKAVANFFSGSCAPCADGTDFPQLCQLCPGCGCSTL
NQYFGYSGAFKCLKDGAGDVAFVKHSTIFENLANKADRDQYELLCLDNTRKPVDEYKDCH
LAQVPSHTVVARSMGGKEDLIWELLNQAQEHFGKDKSKEFQLFSSPHGKDLLFKDSAHGF
LKVPPRMDAKMYLGYEYVTAIRNLREGTC

Ligands and cofactors

IDNameFormulaCopies
CO3Carbonate ionC O31
FEFE (III) ionFe1

Primary citation

Two high-resolution crystal structures of the recombinant N-lobe of human transferrin reveal a structural change implicated in iron release. MacGillivray, R.T., Moore, S.A., Chen, J. et al. Biochemistry (1998) 37:7919-7928. DOI 10.1021/bi980355j · PubMed

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

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