Research workbench
Crystal structure of VAT(D) (form I)
Analyse Crystal structure of VAT(D) (form I) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1KK6
- Type
- protein
- Length
- 619 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Streptogramin a acetyltransferase
- EC
- 2.3.1.-
- UniProt
- P50870
- Pockets
- 4 · best druggability 0.75
Structure
x-ray diffraction · 2 distinct chains · 25% helix, 21% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Streptogramin a acetyltransferase (EC 2.3.1.-) | protein | 207 | 27% helix, 21% strand | P50870 |
| C | Streptogramin a acetyltransferase (EC 2.3.1.-) | protein | 205 | 24% helix, 21% strand | P50870 |
Pockets
4 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 618 | 0.75 | 0.81 | 58 | empty |
| 2 | 548 | 0.72 | 0.80 | 60 | empty |
| 3 | 531 | 0.72 | 0.80 | 54 | empty |
| 4 | 568 | 0.69 | 0.78 | 54 | empty |
Interfaces
3 interfaces between chains.
- B–C · 1349 Ų buried · 12 hydrogen bonds · protein-protein
- A–C · 1347 Ų buried · 14 hydrogen bonds · protein-protein
- A–B · 1330 Ų buried · 11 hydrogen bonds · protein-protein
Compared structures
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 P50870
- Elsewhere: RCSB PDB 1KK6 · PDBe 1KK6 · UniProt P50870
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