Research workbench
Crystal structure of the SVS_A2 protein (205-dremh-209 /205-aqdle-209 mutant) from ancestral sequence reconstruction at 2.38 a resolution
Analyse Crystal structure of the SVS_A2 protein (205-dremh-209 /205-aqdle-209 mutant)… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6TIV
- Type
- protein
- Length
- 654 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Svs variant AT2
- EC
- 4.2.3.158
- Pockets
- 8 · best druggability 0.75
Structure
x-ray diffraction · 2 distinct chains · 67% helix, 1% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Svs variant AT2 (EC 4.2.3.158) | protein | 331 | 68% helix, 1% strand | — |
| B | Svs variant AT2 (EC 4.2.3.158) | protein | 323 | 67% helix, 1% strand | — |
Ligands and binding sites
- PEG · Di(hydroxyethyl)ether · additive · 11 copies · chains A, B
- PG4 · Tetraethylene glycol · additive · chains A
- EDO · 1,2-ethanediol · additive · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
8 pockets found on a 1 Å grid, 7 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 109 | 0.75 | 0.96 | 27 | PEG |
| 2 | 84 | 0.74 | 0.97 | 29 | PEG |
| 3 | 66 | 0.74 | 0.98 | 25 | empty |
| 4 | 385 | 0.73 | 0.84 | 40 | PG4 |
| 5 | 427 | 0.68 | 0.79 | 42 | PEG |
Interfaces
1 interface between chains.
- A–B · 1906 Ų buried · 27 hydrogen bonds · protein-protein
Compared structures
- 6TIV · Crystal structure of the SVS_A2 protein (205-DREMH-209 /205-AQDLE-209 mutant) from… · 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
- Elsewhere: RCSB PDB 6TIV · PDBe 6TIV
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