8WHL: CLASP2
Crystal structure of CLASP2 in complex with CENP-E. Determined by X-ray diffraction at 3.2 Å resolution. Released 28 Aug 2024.
- Method
- X-ray diffraction
- Resolution
- 3.2 Å
- Organism
- Homo sapiens
- Chains
- 8
- Atoms
- 8,755
- Mol. weight
- 137.07 kDa
- Ligands
- MLA
- Released
- 28 Aug 2024
Explore 8WHL in 3D
Show helices and sheets
RCSB PDB
PDBe
Secondary structure: helices and β-sheets
8WHL contains 62 α-helices and 0 β-strands across 8 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.
Chain A: 14 helices, 0 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 1254-1265 | 12 | |
| α-helix | 1272-1287 | 16 | |
| α-helix | 1291-1308 | 18 | |
| α-helix | 1314-1330 | 17 | |
| α-helix | 1332-1338 | 7 | |
| α-helix | 1339-1349 | 11 | |
| α-helix | 1355-1371 | 17 | |
| α-helix | 1374-1387 | 14 | |
| α-helix | 1388-1389 | 2 | |
| α-helix | 1392-1404 | 13 | |
| α-helix | 1409-1427 | 19 | |
| α-helix | 1432-1449 | 18 | |
| α-helix | 1450-1459 | 10 | |
| α-helix | 1462-1477 | 16 | |
Chain B: 16 helices, 0 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 1254-1265 | 12 | |
| α-helix | 1272-1287 | 16 | |
| α-helix | 1291-1307 | 17 | |
| α-helix | 1308-1310 | 3 | |
| α-helix | 1314-1330 | 17 | |
| α-helix | 1332-1338 | 7 | |
| α-helix | 1339-1348 | 10 | |
| α-helix | 1349-1351 | 3 | |
| α-helix | 1355-1371 | 17 | |
| α-helix | 1374-1387 | 14 | |
| α-helix | 1388-1389 | 2 | |
| α-helix | 1392-1404 | 13 | |
| α-helix | 1409-1427 | 19 | |
| α-helix | 1432-1449 | 18 | |
| α-helix | 1450-1457 | 8 | |
| α-helix | 1462-1477 | 16 | |
Chain C: 14 helices, 0 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 1256-1265 | 10 | |
| α-helix | 1272-1287 | 16 | |
| α-helix | 1294-1308 | 15 | |
| α-helix | 1314-1330 | 17 | |
| α-helix | 1332-1338 | 7 | |
| α-helix | 1339-1349 | 11 | |
| α-helix | 1355-1371 | 17 | |
| α-helix | 1374-1387 | 14 | |
| α-helix | 1388-1389 | 2 | |
| α-helix | 1392-1404 | 13 | |
| α-helix | 1409-1427 | 19 | |
| α-helix | 1432-1449 | 18 | |
| α-helix | 1450-1459 | 10 | |
| α-helix | 1462-1476 | 15 | |
Chain D: 14 helices, 0 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 1255-1265 | 11 | |
| α-helix | 1272-1287 | 16 | |
| α-helix | 1291-1308 | 18 | |
| α-helix | 1314-1330 | 17 | |
| α-helix | 1332-1338 | 7 | |
| α-helix | 1339-1349 | 11 | |
| α-helix | 1355-1371 | 17 | |
| α-helix | 1374-1387 | 14 | |
| α-helix | 1388-1389 | 2 | |
| α-helix | 1392-1404 | 13 | |
| α-helix | 1409-1427 | 19 | |
| α-helix | 1432-1449 | 18 | |
| α-helix | 1450-1457 | 8 | |
| α-helix | 1462-1477 | 16 | |
Chains E and G: 1 helix, 0 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 497-546 | 50 | |
Chains F and H: 1 helix, 0 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 495-547 | 53 | |
Molecules and chains
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|
| CLIP-associating protein 2 | A, B, C, D | protein | 235 | Homo sapiens | O75122 (AlphaFold model) |
| Centromere-associated protein E | E, F, G, H | protein | 66 | Homo sapiens | Q02224 (AlphaFold model) |
Sequence of entity 1 (A, B, C, D), FASTA
>8WHL_1 CLIP-associating protein 2 (chains A, B, C, D)
GPGSEFSLDHSDLVAELLKELSNHNERVEERKIALYELMKLTQEESFSVWDEHFKTILLL
LLETLGDKEPTIRALALKVLREILRHQPARFKNYAELTVMKTLEAHKDPHKEVVRSAEEA
ASVLATSISPEQCIKVLCPIIQTADYPINLAAIKMQTKVIERVSKETLNLLLPEIMPGLI
QGYDNSESSVRKACVFCLVAVHAVIGDELKPHLSQLTGSKMKLLNLYIKRAQTGS
Sequence of entity 2 (E, F, G, H), FASTA
>8WHL_2 Centromere-associated protein E (chains E, F, G, H)
GPGSATKLLNQENIESELNSLRADYDNLVLDYEQLRTEKEEMELKLKEKNDLDEFEALER
KTKKDQ
Ligands and cofactors
| ID | Name | Formula | Copies |
|---|
| MLA | Malonic acid | C3 H4 O4 | 1 |
Water and common crystallization additives (ACT) are not listed.
Primary citation
CLASP-mediated competitive binding in protein condensates directs microtubule growth. Jia, X., Lin, L., Guo, S. et al. Nat Commun (2024) 15:6509-6509. DOI 10.1038/s41467-024-50863-3 · PubMed
Other PDB entries of the same protein (UniProt O75122 (AlphaFold model), which also has an AlphaFold model), best resolution first:
- 5NR4 1.2 Å, Crystal structure of Clasp2 TOG1 domain
- 8WHJ 1.4 Å, Crystal structure of CLASP2 TOG4 fused with LL5beta
- 8WHI 1.85 Å, Crystal structure of native CLASP2 in complex with CLIP170
- 3WOY 2.1 Å, Crystal structure of CLASP2 TOG domain (TOG2)
- 8WHK 2.4 Å, Crystal structure of CLASP2 in complex with LL5beta
- 8WHH 3.8 Å, Crystal structure of Se-Met derivative CLASP2 in complex with CLIP170
Browse structure collections
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