Crystal structure of a bonsai version of the human Ndc80 complex. Determined by X-ray diffraction at 2.88 Å resolution. Released 13 May 2008.
Explore 2VE7 in 3D Show helices and sheets RCSB PDB PDBe
2VE7 contains 48 α-helices and 17 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 | 89-105 | 17 | |
| α-helix | 115-117 | 3 | |
| α-helix | 122-133 | 12 | |
| α-helix | 147-157 | 11 | |
| α-helix | 166-170 | 5 | |
| α-helix | 178-200 | 23 | |
| β-strand | 214 | 1 | 1 |
| β-strand | 220 | 1 | 1 |
| α-helix | 222-238 | 17 | |
| α-helix | 244-258 | 15 | |
| α-helix | 264-1125 | 31 | |
| α-helix | 1131-1141 | 11 | |
| α-helix | 1216-1219 | 4 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 89-105 | 17 | |
| α-helix | 122-134 | 13 | |
| α-helix | 147-157 | 11 | |
| α-helix | 166-170 | 5 | |
| α-helix | 178-198 | 21 | |
| β-strand | 214 | 1 | 2 |
| β-strand | 220 | 1 | 2 |
| α-helix | 222-236 | 15 | |
| α-helix | 244-257 | 14 | |
| α-helix | 272-1141 | 39 | |
| β-strand | 1144-1147 | 4 | 3 |
| β-strand | 1154-1158 | 5 | 3 |
| β-strand | 1162 | 1 | 4 |
| β-strand | 1165 | 1 | 4 |
| β-strand | 1170-1175 | 6 | 3 |
| β-strand | 1182-1183 | 2 | 3 |
| α-helix | 1195-1203 | 9 | |
| α-helix | 1207-1221 | 15 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 5-7 | 3 | |
| α-helix | 11-21 | 11 | |
| α-helix | 25-29 | 5 | |
| α-helix | 33-35 | 3 | |
| α-helix | 42-57 | 16 | |
| α-helix | 62-64 | 3 | |
| α-helix | 76-79 | 4 | |
| α-helix | 83-98 | 16 | |
| α-helix | 106-110 | 5 | |
| α-helix | 114-144 | 31 | |
| α-helix | 147-164 | 18 | |
| α-helix | 1137-1147 | 11 | |
| β-strand | 1150-1151 | 2 | 5 |
| β-strand | 1160-1163 | 4 | 5 |
| β-strand | 1172-1175 | 4 | 5 |
| α-helix | 1182-1190 | 9 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 11-21 | 11 | |
| α-helix | 26-30 | 5 | |
| α-helix | 33-35 | 3 | |
| α-helix | 42-57 | 16 | |
| α-helix | 61-65 | 5 | |
| α-helix | 66-68 | 3 | |
| α-helix | 76-79 | 4 | |
| α-helix | 83-98 | 16 | |
| α-helix | 106-110 | 5 | |
| α-helix | 114-148 | 35 | |
| α-helix | 150-1122 | 21 | |
| α-helix | 1127-1131 | 5 | |
| α-helix | 1132-1147 | 16 | |
| β-strand | 1149-1152 | 4 | 6 |
| β-strand | 1160-1165 | 6 | 6 |
| β-strand | 1170-1171 | 2 | 6 |
| β-strand | 1174-1175 | 2 | 6 |
| α-helix | 1182-1191 | 10 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Kinetochore protein HEC1, kinetochore protein SPC25 | A, B | protein | 315 | HOMO SAPIENS | O14777 (AlphaFold model), Q9HBM1 (AlphaFold model) |
| Kinetochore protein NUF2, kinetochore protein SPC24 | C, D | protein | 250 | HOMO SAPIENS | Q8NBT2 (AlphaFold model), Q9BZD4 (AlphaFold model) |
>2VE7_1 KINETOCHORE PROTEIN HEC1, KINETOCHORE PROTEIN SPC25 (chains A, B) MIKDPRPLNDKAFIQQCIRQLCEFLTENGYAHNVSMKSLQAPSVKDFLKIFTFLYGFLCP SYELPDTKFEEEVPRIFKDLGYPFALSKSSMYTVGAPHTWPHIVAALVWLIDCIKIHTAM KESSPLFDDGQPWGEETEDGIMHNKLFLDYTIKCYESFMSGADSFDEMNAELQSKLKDLF NVDAFKLESLEAKNRALNEQIARLEQERSTANKANAERLKRLQKSADLYKDRLGLEIRKI YGEKLQFIFTNIDPKNPESPFMFSLHLNEARDYEVSDSAPHLEGLAEFQENVRKTNNFSA FLANVRKAFTATVYQ
>2VE7_2 KINETOCHORE PROTEIN NUF2, KINETOCHORE PROTEIN SPC24 (chains C, D) GPLGSMETLSFPRYNVAEIVIHIRNKILTGADGKNLTKNDLYPNPKPEVLHMIYMRALQI VYGIRLEHFYMMPVNSGVMYPHLMEGFLPFSNLVTHLDSFLPICRVNDFETADILCPKAK RTSRFLSGIINFIHFREACRETYMEFLWQYKSSADKMQQLNAAHQEALMKLERLEKEVDE DTTVTIPSAVYVAQLYHQVSKIEWEYECEPGMVKGIHHGPSVAQPIHLDSTQLSRKFISD YLWSLVDTEW
| ID | Name | Formula | Copies |
|---|---|---|---|
| IPH | Phenol | C6 H6 O | 2 |
Water and common crystallization additives (GOL) are not listed.
Implications for Kinetochore-Microtubule Attachment from the Structure of an Engineered Ndc80 Complex. Ciferri, C., Pasqualato, S., Screpanti, E. et al. Cell (2008) 133:427. DOI 10.1016/J.CELL.2008.03.020 · PubMed
Other PDB entries of the same protein (UniProt O14777 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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