MolNFT v1 · #153143 · protein
Structural basis of tubulin detyrosination by vasohibins-svbp enzyme complex and functional implications
6J4U · Tubulinyl-tyr carboxypeptidase 1: “Structural basis of tubulin detyrosination by vasohibins-svbp enzyme complex and functional implications”. X-ray diffraction, 2 pockets (best druggability 0.44). MolNFT v1 #153143 on GenesisL1: 3D…
- PDB
- 6J4U
- Type
- protein
- Length
- 276 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Tubulinyl-tyr carboxypeptidase 1; Small vasohibin-binding protein
- EC
- 3.4.17.17
- UniProt
- Q7L8A9, Q8N300
- Pockets
- 2 · best druggability 0.44
Structure
x-ray diffraction · 2 distinct chains · 45% helix, 18% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Tubulinyl-tyr carboxypeptidase 1 (EC 3.4.17.17) | protein | 247 | 41% helix, 20% strand | Q7L8A9 |
| B | Small vasohibin-binding protein | protein | 29 | 83% helix, 0% strand | Q8N300 |
Pockets
2 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 106 | 0.44 | 0.78 | 15 | empty |
| 2 | 53 | 0.25 | 0.73 | 12 | empty |
Interfaces
1 interface between chains.
- A–B · 1184 Ų buried · 17 hydrogen bonds · protein-protein
Compared structures
- 6J4U · Structural basis of tubulin detyrosination by vasohibins-SVBP enzyme complex and… · the same entry in another collection · chain A against A, TM-score 1.00
- Q7L8A9 · AlphaFold monomer V2.0 prediction for tubulinyl-tyr carboxypeptidase 1 (Q7L8A9) · a predicted model of the same protein · chain A against A, TM-score 0.98
- Q8N300 · AlphaFold monomer V2.0 prediction for small vasohibin-binding protein (Q8N300) · a predicted model of the same protein · chain B against A, TM-score 0.81
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 Q7L8A9
- Every structure of UniProt Q8N300
- Elsewhere: RCSB PDB 6J4U · PDBe 6J4U · UniProt Q7L8A9 · UniProt Q8N300
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