Research workbench
Camp-binding acyltransferase from mycobacterium smegmatis
Analyse Camp-binding acyltransferase from mycobacterium smegmatis in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4OLL
- Type
- protein
- Length
- 316 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Acetyltransferase pat
- EC
- 2.3.1.-
- UniProt
- A0R3F9
- Ligands
- CA, HG
- Pockets
- 4 · best druggability 0.72
Structure
x-ray diffraction · 1 distinct chain · 34% helix, 26% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Acetyltransferase pat (EC 2.3.1.-) | protein | 316 | 34% helix, 26% strand | A0R3F9 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
4 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 310 | 0.72 | 0.85 | 32 | empty |
| 2 | 90 | 0.47 | 0.80 | 17 | empty |
| 3 | 71 | 0.36 | 0.77 | 14 | empty |
| 4 | 54 | 0.35 | 0.79 | 16 | empty |
Modifications
Observed in the structure: 9 modified (engineered).
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 A0R3F9
- Elsewhere: RCSB PDB 4OLL · PDBe 4OLL · UniProt A0R3F9
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