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Crystal structure of streptococcus pneumoniae acyl carrier protein synthase (native 2)
Analyse Crystal structure of streptococcus pneumoniae acyl carrier protein synthase… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1FTF
- Type
- protein
- Length
- 342 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Acyl carrier protein synthase
- EC
- 2.7.8.7
- UniProt
- P0A2W6
- Pockets
- 4 · best druggability 0.77
Structure
x-ray diffraction · 2 distinct chains · 45% helix, 32% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Acyl carrier protein synthase (EC 2.7.8.7) | protein | 116 | 46% helix, 31% strand | P0A2W6 |
| C | Acyl carrier protein synthase (EC 2.7.8.7) | protein | 110 | 45% helix, 33% strand | P0A2W6 |
Pockets
4 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 77 | 0.77 | 0.99 | 21 | empty |
| 2 | 325 | 0.56 | 0.75 | 42 | empty |
| 3 | 303 | 0.54 | 0.75 | 39 | empty |
| 4 | 224 | 0.48 | 0.74 | 33 | empty |
Interfaces
3 interfaces between chains.
- A–B · 705 Ų buried · 6 hydrogen bonds · protein-protein
- A–C · 703 Ų buried · 10 hydrogen bonds · protein-protein
- B–C · 671 Ų buried · 5 hydrogen bonds · protein-protein
Compared structures
- 1FTF · Crystal structure of streptococcus pneumoniae acyl carrier protein synthase (native 2) · the same entry in another collection · chain A against A, TM-score 1.00
- P0A2W6 · AlphaFold monomer V2.0 prediction for holo-[acyl-carrier-protein] synthase (P0A2W6) · a predicted model of the same protein · chain C against A, TM-score 0.99
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 P0A2W6
- Elsewhere: RCSB PDB 1FTF · PDBe 1FTF · UniProt P0A2W6
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