Human serum transferrin, recombinant N-terminal lobe. Determined by X-ray diffraction at 1.6 Å resolution. Released 17 Jun 1998.
Explore 1A8E in 3D Show helices and sheets RCSB PDB PDBe
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.
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 4-11 | 8 | 1 |
| α-helix | 12-29 | 18 | |
| β-strand | 35-42 | 8 | 1 |
| α-helix | 45-53 | 9 | |
| β-strand | 59 | 1 | 1 |
| β-strand | 60-62 | 3 | 2 |
| α-helix | 64-71 | 8 | |
| β-strand | 77-84 | 8 | 2 |
| β-strand | 85 | 1 | 3 |
| β-strand | 92 | 1 | 3 |
| β-strand | 94-102 | 9 | 4 |
| α-helix | 109-111 | 3 | |
| β-strand | 117-119 | 3 | 4 |
| α-helix | 125-129 | 5 | |
| α-helix | 130-135 | 6 | |
| α-helix | 136-138 | 3 | |
| α-helix | 140 | 1 | |
| α-helix | 142 | 1 | |
| α-helix | 146-153 | 8 | |
| β-strand | 157-158 | 2 | 4 |
| α-helix | 168-171 | 4 | |
| α-helix | 187-196 | 10 | |
| β-strand | 202-206 | 5 | 4 |
| α-helix | 209-213 | 5 | |
| α-helix | 217-220 | 4 | |
| β-strand | 223-227 | 5 | 4 |
| β-strand | 231-234 | 4 | 4 |
| α-helix | 235-240 | 6 | |
| β-strand | 244-247 | 4 | 4 |
| α-helix | 248-249 | 2 | |
| β-strand | 250-254 | 5 | 2 |
| α-helix | 260-274 | 15 | |
| β-strand | 301-304 | 4 | 2 |
| α-helix | 305-306 | 2 | |
| α-helix | 311-315 | 5 | |
| α-helix | 317-327 | 11 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Serum transferrin | A | protein | 329 | Homo sapiens | P02787 (AlphaFold model) |
>1A8E_1 SERUM TRANSFERRIN (chains A) DKTVRWCAVSEHEATKCQSFRDHMKSVIPSDGPSVACVKKASYLDCIRAIAANEADAVTL DAGLVYDAYLAPNNLKPVVAEFYGSKEDPQTFYYAVAVVKKDSGFQMNQLRGKKSCHTGL GRSAGWNIPIGLLYCDLPEPRKPLEKAVANFFSGSCAPCADGTDFPQLCQLCPGCGCSTL NQYFGYSGAFKCLKDGAGDVAFVKHSTIFENLANKADRDQYELLCLDNTRKPVDEYKDCH LAQVPSHTVVARSMGGKEDLIWELLNQAQEHFGKDKSKEFQLFSSPHGKDLLFKDSAHGF LKVPPRMDAKMYLGYEYVTAIRNLREGTC
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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