Research workbench
Crystal structure of human EB1 in complex with microtubule tip localization signal peptide of macf
Analyse Crystal structure of human EB1 in complex with microtubule tip localization… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3GJO
- Type
- protein
- Length
- 282 residues
- Chains
- 8
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Microtubule-associated protein RP/EB family member 1; Dystonin
- UniProt
- Q15691, Q5TBT1
- Pockets
- 2 · best druggability 0.54
Structure
x-ray diffraction · 8 distinct chains · 68% helix, 4% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Microtubule-associated protein RP/EB family member 1 | protein | 66 | 73% helix, 3% strand | Q15691 |
| B | Microtubule-associated protein RP/EB family member 1 | protein | 64 | 75% helix, 2% strand | Q15691 |
| C | Microtubule-associated protein RP/EB family member 1 | protein | 65 | 72% helix, 3% strand | Q15691 |
| D | Microtubule-associated protein RP/EB family member 1 | protein | 54 | 89% helix, 0% strand | Q15691 |
| E | Dystonin | protein | 11 | 0% helix, 18% strand | Q5TBT1 |
| F | Dystonin | protein | 9 | 0% helix, 11% strand | Q5TBT1 |
| G | Dystonin | protein | 8 | 0% helix, 25% strand | Q5TBT1 |
| H | Dystonin | protein | 5 | 0% helix, 0% strand | Q5TBT1 |
Pockets
2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 328 | 0.54 | 0.74 | 36 | empty |
| 2 | 96 | 0.34 | 0.73 | 20 | empty |
Interfaces
15 interfaces between chains.
- A–B · 1754 Ų buried · 8 hydrogen bonds · protein-protein
- C–D · 1692 Ų buried · 11 hydrogen bonds · protein-protein
- A–E · 594 Ų buried · 7 hydrogen bonds · protein-protein
- C–G · 583 Ų buried · 4 hydrogen bonds · protein-protein
- B–F · 540 Ų buried · 7 hydrogen bonds · protein-protein
Compared structures
- 3GJO · Crystal structure of human EB1 in complex with microtubule Tip localization signal… · the same entry in another collection · chain H against H, 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 B against A, TM-score 0.88
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
- Every structure of UniProt Q5TBT1
- Elsewhere: RCSB PDB 3GJO · PDBe 3GJO · UniProt Q15691 · UniProt Q5TBT1
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