Structure of camel apo-lactoferrin demonstrates its dual role in sequestering and transporting ferric ions simultaneously:crystal structure of camel apo-lactoferrin at 2.6A resolution. Determined by X-ray diffraction at 2.65 Å resolution. Released 20 Jun 2001.
Explore 1DTZ in 3D Show helices and sheets RCSB PDB PDBe
1DTZ contains 32 α-helices and 34 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 | 6-10 | 5 | 1 |
| α-helix | 13-27 | 15 | |
| β-strand | 34-38 | 5 | 1 |
| α-helix | 42-50 | 9 | |
| β-strand | 56 | 1 | 1 |
| β-strand | 57-59 | 3 | 2 |
| α-helix | 61-68 | 8 | |
| β-strand | 74-80 | 7 | 2 |
| β-strand | 82 | 1 | 3 |
| β-strand | 89 | 1 | 3 |
| β-strand | 91-99 | 9 | 4 |
| α-helix | 106-108 | 3 | |
| β-strand | 113-116 | 4 | 4 |
| α-helix | 122-126 | 5 | |
| α-helix | 127-131 | 5 | |
| α-helix | 133-135 | 3 | |
| α-helix | 145-152 | 8 | |
| β-strand | 155-157 | 3 | 4 |
| α-helix | 167-170 | 4 | |
| α-helix | 177-179 | 3 | |
| α-helix | 191-200 | 10 | |
| β-strand | 206-210 | 5 | 4 |
| α-helix | 213-217 | 5 | |
| α-helix | 221-224 | 4 | |
| β-strand | 227-231 | 5 | 4 |
| β-strand | 235-237 | 3 | 4 |
| α-helix | 239-241 | 3 | |
| β-strand | 248-251 | 4 | 4 |
| α-helix | 252-253 | 2 | |
| β-strand | 254-258 | 5 | 2 |
| α-helix | 264-278 | 15 | |
| β-strand | 307-309 | 3 | 2 |
| α-helix | 310-311 | 2 | |
| α-helix | 316-320 | 5 | |
| α-helix | 322-329 | 8 | |
| α-helix | 335-343 | 9 | |
| β-strand | 345-350 | 6 | 5 |
| α-helix | 352-365 | 14 | |
| β-strand | 369-374 | 6 | 5 |
| α-helix | 377-385 | 9 | |
| β-strand | 391 | 1 | 5 |
| β-strand | 392-394 | 3 | 6 |
| α-helix | 396-403 | 8 | |
| β-strand | 408-415 | 8 | 6 |
| α-helix | 433 | 1 | |
| β-strand | 434 | 1 | 7 |
| β-strand | 435-438 | 4 | 8 |
| β-strand | 439-440 | 2 | 9 |
| β-strand | 455-458 | 4 | 8 |
| β-strand | 489-491 | 3 | 8 |
| β-strand | 502 | 1 | 8 |
| β-strand | 508 | 1 | 10 |
| β-strand | 512 | 1 | 10 |
| α-helix | 525-534 | 10 | |
| β-strand | 540-544 | 5 | 8 |
| α-helix | 545-548 | 4 | |
| β-strand | 569-570 | 2 | 9 |
| α-helix | 581-586 | 6 | |
| β-strand | 591 | 1 | 7 |
| α-helix | 592-595 | 4 | |
| β-strand | 596-599 | 4 | 6 |
| α-helix | 604-618 | 15 | |
| β-strand | 645-650 | 6 | 6 |
| α-helix | 657-661 | 5 | |
| α-helix | 663-673 | 11 | |
| α-helix | 679-686 | 8 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Apo lactoferrin | A | protein | 689 | Camelus dromedarius | Q9TUM0 (AlphaFold model) |
>1DTZ_1 APO LACTOFERRIN (chains A) ASKKSVRWCTTSPAESKKCAQWQRRMKKVRGPSVTCVKKTSRFECIQAISTEKADAVTLD GGLVYDAGLDPYKLRPIAAEVYGTENQPQTHYYAVAIAKKGTNFQLNQLQGLKSCHTGLG RSAGWNIPMGLLRPFLDWTGPPEPLQKAVAKFFSASCVPCVDGKEYPNLCQLCAGTGENK CACSSQEPYFGYSGAFKCLQDGAGDVAFVKDSTVFESLPAKADRDQYELLCPNNTRKPVD AFQECHLARVPSHAVVARSVNGKEDLIWKLLVKAQEKFGRGKPSAFQLFGSPAGQKDLLF KDSALGLLRIPKKIDSGLYLGSNYITAIRGLRETAAEVELRRAQVVWCAVGSDEQLKCQE WSRQSNQSVVCATASTTEDCIALVLKGEADALSLDGGYIYIAGKCGLVPVLAESQQSPES SGLDCVHRPVKGYLAVAVVRKANDKITWNSLRGKKSCHTAVDRTAGWNIPMGPLFKDTDS CRFDEFFSQSCAPGSDPRSKLCALCAGNEEGQLKCVPNSSERLYGYTGAFRCLAENVGDV AFVKDVTVLDNTDGKGTEQWAKDLKLGDFELLCLNGTRKPVTEAESCHLPVAPNHAVVSR IDKVAHLRQVLLRQQAHFGRNGEDCPGKFCLFQSKTKNLLFNDNTECLAKLQGKTTYDEY LGPQYVTAIAKLRRCSTSPLLEACAFLMR
Camel lactoferrin, a transferrin-cum-lactoferrin: crystal structure of camel apolactoferrin at 2.6 A resolution and structural basis of its dual role. Khan, J.A., Kumar, P., Paramasivam, M. et al. J Mol Biol (2001) 309:751-761. DOI 10.1006/jmbi.2001.4692 · PubMed
Other PDB entries of the same protein (UniProt Q9TUM0 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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