Research workbench
Structure of E. COLI FABF(C163Q) in complex with dihydrophenyl platensimycin
Analyse Structure of E. COLI FABF(C163Q) in complex with dihydrophenyl platensimycin in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3G11
- Type
- protein
- Length
- 411 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- 3-oxoacyl-[acyl-carrier-protein] synthase 2
- EC
- 2.3.1.179
- UniProt
- P0AAI5
- Ligands
- P9C
- Pockets
- 3 · best druggability 0.74
Structure
x-ray diffraction · 1 distinct chain · 39% helix, 21% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | 3-oxoacyl-[acyl-carrier-protein] synthase 2 (EC 2.3.1.179) | protein | 411 | 39% helix, 21% strand | P0AAI5 |
Ligands and binding sites
- P9C · 3-({3-[(1S,4S,4aS,6S,7S,9S,9aR)-1,6-dimethyl-2-oxo-4-phenyldecahydro-6,9-epoxy-4a,7-methanobenzo[7]annulen-1-yl]propanoyl}amino)-2,4-dihydroxybenzoic acid · ligand · 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 | 188 | 0.74 | 0.90 | 36 | P9C |
| 2 | 59 | 0.36 | 0.79 | 14 | empty |
| 3 | 55 | 0.33 | 0.77 | 19 | empty |
Compared structures
- 3G11 · Structure of E. coli FabF(C163Q) in complex with dihydrophenyl platensimycin · the same entry in another collection · chain A against A, TM-score 1.00
- P0AAI5 · AlphaFold monomer V2.0 prediction for 3-oxoacyl-[acyl-carrier- protein] synthase 2… · a predicted model of the same protein · 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 P0AAI5
- Elsewhere: RCSB PDB 3G11 · PDBe 3G11 · UniProt P0AAI5
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