Research workbench
Structure of E.COLI fabd complexed with malonate
Analyse Structure of E.COLI fabd complexed with malonate in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2G2Y
- Type
- protein
- Length
- 305 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Malonyl CoA-acyl carrier protein transacylase
- EC
- 2.3.1.39
- UniProt
- P0AAI9
- Pockets
- 1 · best druggability 0.64
Structure
x-ray diffraction · 1 distinct chain · 51% helix, 15% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Malonyl CoA-acyl carrier protein transacylase (EC 2.3.1.39) | protein | 305 | 51% helix, 15% strand | P0AAI9 |
Ligands and binding sites
- MLI · Malonate ion · additive · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 353 | 0.64 | 0.79 | 37 | MLI |
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 P0AAI9
- Elsewhere: RCSB PDB 2G2Y · PDBe 2G2Y · UniProt P0AAI9
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