Crystal structure of botrocetin. Determined by X-ray diffraction at 1.8 Å resolution. Released 14 Feb 2001.
Explore 1FVU in 3D Show helices and sheets RCSB PDB PDBe
1FVU contains 21 α-helices and 36 β-strands across 4 chains. 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 | 6 | 1 | |
| β-strand | 7-9 | 3 | 1 |
| β-strand | 12-21 | 10 | 1 |
| α-helix | 23-33 | 11 | |
| β-strand | 38-39 | 2 | 1 |
| α-helix | 48-59 | 12 | |
| β-strand | 66-73 | 8 | 1 |
| β-strand | 83 | 1 | 2 |
| α-helix | 88 | 1 | |
| β-strand | 89 | 1 | 2 |
| α-helix | 90 | 1 | |
| β-strand | 95 | 1 | 3 |
| α-helix | 97-99 | 3 | |
| β-strand | 103-107 | 5 | 1 |
| β-strand | 115-118 | 4 | 1 |
| β-strand | 124-130 | 7 | 1 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 402 | 1 | |
| β-strand | 407-409 | 3 | 3 |
| β-strand | 412-421 | 10 | 3 |
| α-helix | 423-433 | 11 | |
| β-strand | 438-439 | 2 | 3 |
| α-helix | 445-452 | 8 | |
| α-helix | 459 | 1 | |
| β-strand | 464-465 | 2 | 3 |
| β-strand | 477-479 | 3 | 1 |
| α-helix | 483-485 | 3 | |
| β-strand | 497-502 | 6 | 3 |
| β-strand | 507-512 | 6 | 3 |
| β-strand | 517-523 | 7 | 3 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 202-203 | 2 | |
| β-strand | 207-209 | 3 | 4 |
| β-strand | 212-221 | 10 | 4 |
| α-helix | 223-233 | 11 | |
| β-strand | 238-239 | 2 | 4 |
| α-helix | 248-257 | 10 | |
| β-strand | 266-273 | 8 | 4 |
| β-strand | 283 | 1 | 5 |
| α-helix | 288 | 1 | |
| β-strand | 289 | 1 | 5 |
| α-helix | 290 | 1 | |
| β-strand | 295 | 1 | 6 |
| α-helix | 297-299 | 3 | |
| β-strand | 303-307 | 5 | 4 |
| β-strand | 315-318 | 4 | 4 |
| β-strand | 324-330 | 7 | 4 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 602-603 | 2 | |
| β-strand | 607-609 | 3 | 6 |
| β-strand | 612-621 | 10 | 6 |
| α-helix | 623-631 | 9 | |
| β-strand | 638-639 | 2 | 6 |
| α-helix | 645-652 | 8 | |
| β-strand | 664-669 | 6 | 6 |
| β-strand | 677-679 | 3 | 4 |
| α-helix | 683-685 | 3 | |
| β-strand | 697-702 | 6 | 6 |
| β-strand | 707-712 | 6 | 6 |
| β-strand | 717-724 | 8 | 6 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Botrocetin alpha chain | A, C | protein | 133 | Bothrops jararaca | P22029 (AlphaFold model) |
| Botrocetin beta chain | B, D | protein | 125 | Bothrops jararaca | P22030 (AlphaFold model) |
>1FVU_1 BOTROCETIN ALPHA CHAIN (chains A, C) DCPSGWSSYEGNCYKFFQQKMNWADAERFCSEQAKGGHLVSIKIYSKEKDFVGDLVTKNI QSSDLYAWIGLRVENKEKQCSSEWSDGSSVSYENVVERTVKKCFALEKDLGFVLWINLYC AQKNPFVCKSPPP
>1FVU_2 BOTROCETIN BETA CHAIN (chains B, D) DCPPDWSSYEGHCYRFFKEWMHWDDAEEFCTEQQTGAHLVSFQSKEEADFVRSLTSEMLK GDVVWIGLSDVWNKCRFEWTDGMEFDYDDYYLIAEYECVASKPTNNKWWIIPCTRFKNFV CEFQA
| ID | Name | Formula | Copies |
|---|---|---|---|
| MG | Magnesium ion | Mg | 2 |
Crystal structure of the von Willebrand factor modulator botrocetin. Sen, U., Vasudevan, S., Subbarao, G. et al. Biochemistry (2001) 40:345-352. DOI 10.1021/bi0021737 · PubMed
Other PDB entries of the same protein (UniProt P22029 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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