Research workbench
Structure of the acyl transferase domain of zmaa
Analyse Structure of the acyl transferase domain of zmaa in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4QBU
- Type
- protein
- Length
- 436 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Zmaa
- UniProt
- C0JRE5
- Pockets
- 3 · best druggability 0.72
Structure
x-ray diffraction · 1 distinct chain · 48% helix, 13% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Zmaa | protein | 436 | 48% helix, 13% strand | C0JRE5 |
Ligands and binding sites
- FMT · Formic acid · additive · chains A
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 | 510 | 0.72 | 0.81 | 58 | FMT |
| 2 | 129 | 0.41 | 0.75 | 19 | empty |
| 3 | 53 | 0.36 | 0.80 | 16 | empty |
Compared structures
- 4QBU · Structure of the Acyl Transferase domain of ZmaA · 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 C0JRE5
- Elsewhere: RCSB PDB 4QBU · PDBe 4QBU · UniProt C0JRE5
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