Research workbench
Structure of HACF7 EF1-EF2-gar domains
Analyse Structure of HACF7 EF1-EF2-gar domains in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5VE9
- Type
- protein
- Length
- 253 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Microtubule-actin cross-linking factor 1, isoforms 1/2/3/5
- UniProt
- Q9UPN3
- Ligands
- CA, ZN
- Pockets
- 3 · best druggability 0.52
Structure
x-ray diffraction · 3 distinct chains · 48% helix, 18% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Microtubule-actin cross-linking factor 1, isoforms 1/2/3/5 | protein | 88 | 58% helix, 11% strand | Q9UPN3 |
| C | Microtubule-actin cross-linking factor 1, isoforms 1/2/3/5 | protein | 74 | 28% helix, 35% strand | Q9UPN3 |
| B | Microtubule-actin cross-linking factor 1, isoforms 1/2/3/5 | protein | 91 | 55% helix, 11% strand | Q9UPN3 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 199 | 0.52 | 0.77 | 24 | empty |
| 2 | 101 | 0.44 | 0.79 | 23 | empty |
| 3 | 55 | 0.24 | 0.72 | 18 | empty |
Interfaces
3 interfaces between chains.
- A–B · 1070 Ų buried · 15 hydrogen bonds · protein-protein
- C–B · 479 Ų buried · 6 hydrogen bonds · protein-protein
- A–C · 342 Ų buried · 5 hydrogen bonds · protein-protein
Compared structures
- 5VE9 · Structure of hACF7 EF1-EF2-GAR domains · 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 Q9UPN3
- Elsewhere: RCSB PDB 5VE9 · PDBe 5VE9 · UniProt Q9UPN3
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