Crystal Structure of High-Affinity von Willebrand Factor A1 domain with Disulfide Mutation. Determined by X-ray diffraction at 2.2 Å resolution. Released 8 Jan 2014.
Explore 4C29 in 3D Show helices and sheets RCSB PDB PDBe
4C29 contains 28 α-helices and 22 β-strands across 2 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 |
|---|---|---|---|
| β-strand | 1274 | 1 | 1 |
| β-strand | 1276-1283 | 8 | 2 |
| β-strand | 1285 | 1 | 3 |
| α-helix | 1290-1305 | 16 | |
| β-strand | 1309 | 1 | 2 |
| β-strand | 1314-1321 | 8 | 2 |
| β-strand | 1325-1329 | 5 | 2 |
| α-helix | 1337-1345 | 9 | |
| α-helix | 1347-1349 | 3 | |
| β-strand | 1352 | 1 | 3 |
| α-helix | 1357-1363 | 7 | |
| α-helix | 1364-1368 | 5 | |
| β-strand | 1378-1385 | 8 | 2 |
| α-helix | 1391-1394 | 4 | |
| α-helix | 1397-1406 | 10 | |
| β-strand | 1409-1416 | 8 | 2 |
| α-helix | 1422-1429 | 8 | |
| α-helix | 1433-1435 | 3 | |
| α-helix | 1436-1437 | 2 | |
| β-strand | 1438-1440 | 3 | 2 |
| α-helix | 1443-1445 | 3 | |
| α-helix | 1446-1460 | 15 | |
| α-helix | 1462 | 1 | |
| β-strand | 1463 | 1 | 1 |
| α-helix | 1464-1465 | 2 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 1274 | 1 | 4 |
| β-strand | 1276-1283 | 8 | 5 |
| β-strand | 1285 | 1 | 6 |
| α-helix | 1290-1305 | 16 | |
| β-strand | 1309 | 1 | 5 |
| β-strand | 1314-1321 | 8 | 5 |
| β-strand | 1325-1329 | 5 | 5 |
| α-helix | 1337-1345 | 9 | |
| α-helix | 1347-1349 | 3 | |
| β-strand | 1352 | 1 | 6 |
| α-helix | 1357-1363 | 7 | |
| α-helix | 1364-1368 | 5 | |
| β-strand | 1378-1385 | 8 | 5 |
| α-helix | 1391-1393 | 3 | |
| α-helix | 1397-1406 | 10 | |
| β-strand | 1409-1416 | 8 | 5 |
| α-helix | 1422-1429 | 8 | |
| α-helix | 1433-1435 | 3 | |
| α-helix | 1436-1437 | 2 | |
| β-strand | 1438-1440 | 3 | 5 |
| α-helix | 1443-1445 | 3 | |
| α-helix | 1450-1460 | 11 | |
| α-helix | 1462 | 1 | |
| β-strand | 1463 | 1 | 4 |
| α-helix | 1464-1465 | 2 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Von willebrand factor | A, B | protein | 215 | HOMO SAPIENS | P04275 (AlphaFold model) |
>4C29_1 VON WILLEBRAND FACTOR (chains A, B) MEPPLHDFCRSRLLDLVFLLDGSSRLSEAEFEVLKAFVVDMMERLRISQKWVRVAVVEYH DGSHAYIGLKDRKRPSELRRIASQVKYAGSQVASTSEVLKYTLFQIFSKIDRPEASRIAL LLMASQEPQRMSRNFVRYVQGLKKKKVIVIPVGIGPHANLKQIRLIEKQAPENKAFVLSS VDELEQQRDEIVSYLCDLAPEAPPPTLPPHHHHHH
| ID | Name | Formula | Copies |
|---|---|---|---|
| CA | Calcium ion | Ca | 3 |
Water and common crystallization additives (PEG, ACT) are not listed.
Towards the Structural Basis of Regulation of Von Willebrand Factor Binding to Glycoprotein Ib. Blenner, M.A., Dong, X., Springer, T.A. J Biol Chem (2014) 289:5565. DOI 10.1074/JBC.M113.511220 · PubMed
Other PDB entries of the same protein (UniProt P04275 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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