Research workbench
Crystal structure of the motor domain of human kinetochore protein cenp-E
Analyse Crystal structure of the motor domain of human kinetochore protein cenp-E in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1T5C
- Type
- protein
- Length
- 632 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Centromeric protein E
- UniProt
- Q02224
- Ligands
- ADP, PIN, MG, NO3
- Pockets
- 11 · best druggability 0.65
Structure
x-ray diffraction · 2 distinct chains · 28% helix, 26% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Centromeric protein E | protein | 322 | 29% helix, 28% strand | Q02224 |
| B | Centromeric protein E | protein | 310 | 28% helix, 25% strand | Q02224 |
Ligands and binding sites
- ADP · Adenosine-5'-diphosphate · ligand · 2 copies · chains A, B
- PIN · Piperazine-N,N'-bis(2-ethanesulfonic acid) · ligand · chains A
- MG · Magnesium ion · metal · 2 copies · chains A, B
- NO3 · Nitrate ion · ion · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
11 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 276 | 0.65 | 0.82 | 35 | empty |
| 2 | 293 | 0.63 | 0.80 | 40 | empty |
| 3 | 194 | 0.51 | 0.77 | 28 | empty |
| 4 | 129 | 0.48 | 0.78 | 18 | empty |
| 5 | 96 | 0.42 | 0.78 | 18 | PIN |
Interfaces
1 interface between chains.
- A–B · 457 Ų buried · 10 hydrogen bonds · protein-protein
Compared structures
- 1T5C · Crystal structure of the motor domain of human kinetochore protein CENP-E · the same entry in another collection · chain A against A, TM-score 1.00
Analyse
- Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
- Every structure of UniProt Q02224
- Elsewhere: RCSB PDB 1T5C · PDBe 1T5C · UniProt Q02224
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