Crystal structure of hen serum transferrin in apo- form. Determined by X-ray diffraction at 3.5 Å resolution. Released 13 Jul 2004.
Explore 1RYX in 3D Show helices and sheets RCSB PDB PDBe
1RYX contains 34 α-helices and 29 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 |
|---|---|---|---|
| α-helix | 15-19 | 5 | |
| α-helix | 24-28 | 5 | |
| α-helix | 42-50 | 9 | |
| β-strand | 56-57 | 2 | 1 |
| α-helix | 61-67 | 7 | |
| β-strand | 75-79 | 5 | 1 |
| β-strand | 80-81 | 2 | 2 |
| β-strand | 93-94 | 2 | 3 |
| β-strand | 97 | 1 | 4 |
| β-strand | 99 | 1 | 5 |
| α-helix | 122-126 | 5 | |
| α-helix | 127-129 | 3 | |
| α-helix | 132-135 | 4 | |
| α-helix | 143-145 | 3 | |
| α-helix | 148-153 | 6 | |
| α-helix | 192-198 | 7 | |
| β-strand | 206 | 1 | 4 |
| β-strand | 209 | 1 | 3 |
| α-helix | 213-216 | 4 | |
| β-strand | 224 | 1 | 5 |
| β-strand | 245-246 | 2 | 3 |
| β-strand | 251-254 | 4 | 1 |
| α-helix | 261-274 | 14 | |
| β-strand | 306-307 | 2 | 2 |
| α-helix | 322-330 | 9 | |
| α-helix | 379-386 | 8 | |
| β-strand | 392-394 | 3 | 6 |
| α-helix | 398-405 | 8 | |
| β-strand | 408 | 1 | 7 |
| β-strand | 411 | 1 | 8 |
| β-strand | 412 | 1 | 6 |
| β-strand | 432 | 1 | 9 |
| β-strand | 433-435 | 3 | 10 |
| β-strand | 436-438 | 3 | 11 |
| α-helix | 445-447 | 3 | |
| β-strand | 453-454 | 2 | 12 |
| α-helix | 461-463 | 3 | |
| α-helix | 467-470 | 4 | |
| α-helix | 471-473 | 3 | |
| α-helix | 480-482 | 3 | |
| β-strand | 487-488 | 2 | 12 |
| α-helix | 523-531 | 9 | |
| β-strand | 539-541 | 3 | 10 |
| α-helix | 542-544 | 3 | |
| α-helix | 545-548 | 4 | |
| α-helix | 563-565 | 3 | |
| β-strand | 566-568 | 3 | 11 |
| α-helix | 569-570 | 2 | |
| α-helix | 580-583 | 4 | |
| β-strand | 588 | 1 | 9 |
| α-helix | 589-592 | 4 | |
| β-strand | 593-595 | 3 | 6 |
| β-strand | 596 | 1 | 7 |
| β-strand | 597 | 1 | 13 |
| β-strand | 600 | 1 | 13 |
| α-helix | 606-609 | 4 | |
| α-helix | 620-623 | 4 | |
| α-helix | 645 | 1 | |
| β-strand | 646 | 1 | 8 |
| α-helix | 647-648 | 2 | |
| α-helix | 653-657 | 5 | |
| α-helix | 661-667 | 7 | |
| α-helix | 675-684 | 10 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Ovotransferrin | A | protein | 686 | Gallus gallus | P02789 (AlphaFold model) |
>1RYX_1 Ovotransferrin (chains A) APPKSVIRWCTISSPEEKKCNNLRDLTQQERISLTCVQKATYLDCIKAIANNEADAISLD GGQAFEAGLAPYKLKPIAAEVYEHTEGSTTSYYAVAVVKKGTEFTVNDLQGKTSCHTGLG RSAGWNIPIGTLLHRGAIEWEGIESGSVEQAVAKFFSASCVPGATIEQKLCRQCKGDPKT KCARNAPYSGYSGAFHCLKDGKGDVAFVKHTTVNENAPDQKDEYELLCLDGSRQPVDNYK TCNWARVAAHAVVARDDNKVEDIWSFLSKAQSDFGVDTKSDFHLFGPPGKKDPVLKDLLF KDSAIMLKRVPSLMDSQLYLGFEYYSAIQSMRKDQLTPSPRENRIQWCAVGKDEKSKCDR WSVVSNGDVECTVVDETKDCIIKIMKGEADAVALDGGLVYTAGVCGLVPVMAERYDDESQ CSKTDERPASYFAVAVARKDSNVNWNNLKGKKSCHTAVGRTAGWVIPMGLIHNRTGTCNF DEYFSEGCAPGSPPNSRLCQLCQGSGGIPPEKCVASSHEKYFGYTGALRCLVEKGDVAFI QHSTVEENTGGKNKADWAKNLQMDDFELLCTDGRRANVMDYRECNLAEVPTHAVVVRPEK ANKIRDLLERQEKRFGVNGSEKSKFMMFESQNKDLLFKDLTKCLFKVREGTTYKEFLGDK FYTVISSLKTCNPSDILQMCSFLEGK
Tertiary structural changes associated with iron binding and release in hen serum transferrin: a crystallographic and spectroscopic study. Thakurta, P.G., Choudhury, D., Dasgupta, R. et al. Biochem Biophys Res Commun (2004) 316:1124-1131. DOI 10.1016/j.bbrc.2004.02.165 · PubMed
Other PDB entries of the same protein (UniProt P02789 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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