MolNFT v1 · #50116 · protein
Structure of fragment of human end-binding protein 1 (EB1) containing the N-terminal domain at 1.35 a resolution
2R8U · Microtubule-associated protein RP/EB family member 1: “Structure of fragment of human end-binding protein 1 (EB1) containing the N-terminal domain at 1.35 a…”. X-ray diffraction, 1 ligand (MOO), 5 pockets (best druggability 0.41).…
- PDB
- 2R8U
- Type
- protein
- Length
- 267 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Microtubule-associated protein RP/EB family member 1
- UniProt
- Q15691
- Ligands
- MOO
- Pockets
- 5 · best druggability 0.41
Structure
x-ray diffraction · 2 distinct chains · 56% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Microtubule-associated protein RP/EB family member 1 | protein | 131 | 56% helix, 0% strand | Q15691 |
| B | Microtubule-associated protein RP/EB family member 1 | protein | 136 | 56% helix, 0% strand | Q15691 |
Ligands and binding sites
- MOO · Molybdate ion · ion · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
5 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 88 | 0.41 | 0.78 | 19 | empty |
| 2 | 85 | 0.38 | 0.77 | 17 | empty |
| 3 | 85 | 0.35 | 0.75 | 20 | empty |
| 4 | 50 | 0.29 | 0.76 | 14 | empty |
| 5 | 51 | 0.29 | 0.75 | 13 | MOO |
Interfaces
1 interface between chains.
- A–B · 402 Ų buried · 6 hydrogen bonds · protein-protein
Compared structures
- 2R8U · Structure of fragment of human end-binding protein 1 (EB1) containing the N-terminal… · the same entry in another collection · chain A against A, TM-score 1.00
- Q15691 · AlphaFold monomer V2.0 prediction for microtubule-associated protein RP/EB family member… · a predicted model of the same protein · chain A against A, TM-score 0.97
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 Q15691
- Elsewhere: RCSB PDB 2R8U · PDBe 2R8U · UniProt Q15691
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