Research workbench
Synechococcus olefin synthase faal domain A229I/R336A in complex with palmitoyl adenylate and pyrophosphate
Analyse Synechococcus olefin synthase faal domain A229I/R336A in complex with palmitoyl… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7R7G
- Type
- protein
- Length
- 1,134 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Polyketide synthase
- EC
- 6.2.1.20
- UniProt
- B1XKC6
- Ligands
- 1TF, POP, MG
- Pockets
- 4 · best druggability 0.86
Structure
x-ray diffraction · 1 distinct chain · 35% helix, 27% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Polyketide synthase (EC 6.2.1.20) | protein | 567 | 35% helix, 27% strand | B1XKC6 |
Ligands and binding sites
- 1TF · palmitoyl adenylate · ligand · 2 copies · chains A, B
- POP · Pyrophosphate 2- · ligand · 2 copies · chains A, B
- MG · Magnesium ion · metal · 2 copies · chains A, B
- ACT · Acetate ion · additive · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
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 | 1151 | 0.86 | 0.87 | 127 | 1TF, POP, MG |
| 2 | 1165 | 0.86 | 0.87 | 129 | 1TF, POP, MG |
| 3 | 844 | 0.71 | 0.76 | 51 | ACT |
| 4 | 75 | 0.30 | 0.74 | 14 | empty |
Interfaces
1 interface between chains.
- A–B · 643 Ų buried · 6 hydrogen bonds · protein-protein
Compared structures
- 7R7G · Synechococcus Olefin Synthase FAAL domain A229I/R336A in complex with palmitoyl adenylate… · 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 B1XKC6
- Elsewhere: RCSB PDB 7R7G · PDBe 7R7G · UniProt B1XKC6
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