Research workbench
Crystal structure of sfp aldolase yiht from salmonella enterica in complex with sulfate bound at the active site
Analyse Crystal structure of sfp aldolase yiht from salmonella enterica in complex with… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7AG7
- Type
- protein
- Length
- 3,461 residues
- Chains
- 12
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Sulfofructosephosphate aldolase
- EC
- 4.1.2.57
- UniProt
- Q9L7R9
- Ligands
- SO4
- Pockets
- 20 · best druggability 0.69
Structure
x-ray diffraction · 9 distinct chains · 44% helix, 20% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Sulfofructosephosphate aldolase (EC 4.1.2.57) | protein | 289 | 45% helix, 20% strand | Q9L7R9 |
| B | Sulfofructosephosphate aldolase (EC 4.1.2.57) | protein | 291 | 44% helix, 19% strand | Q9L7R9 |
| C | Sulfofructosephosphate aldolase (EC 4.1.2.57) | protein | 290 | 44% helix, 19% strand | Q9L7R9 |
| D | Sulfofructosephosphate aldolase (EC 4.1.2.57) | protein | 293 | 44% helix, 20% strand | Q9L7R9 |
| E | Sulfofructosephosphate aldolase (EC 4.1.2.57) | protein | 292 | 44% helix, 20% strand | Q9L7R9 |
| F | Sulfofructosephosphate aldolase (EC 4.1.2.57) | protein | 276 | 43% helix, 20% strand | Q9L7R9 |
| G | Sulfofructosephosphate aldolase (EC 4.1.2.57) | protein | 288 | 45% helix, 20% strand | Q9L7R9 |
| H | Sulfofructosephosphate aldolase (EC 4.1.2.57) | protein | 286 | 45% helix, 19% strand | Q9L7R9 |
| I, J, K, L | Sulfofructosephosphate aldolase (EC 4.1.2.57) | protein | 289 | 45% helix, 20% strand | Q9L7R9 |
Ligands and binding sites
- SO4 · Sulfate ion · ion · 12 copies · chains A, B, C, D, E, F, G, H, I, J, K, L
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
20 pockets found on a 1 Å grid, 18 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 446 | 0.69 | 0.80 | 64 | empty |
| 2 | 285 | 0.67 | 0.82 | 41 | SO4 |
| 3 | 277 | 0.66 | 0.82 | 41 | SO4 |
| 4 | 226 | 0.65 | 0.83 | 36 | SO4 |
| 5 | 327 | 0.65 | 0.80 | 53 | SO4 |
Interfaces
17 interfaces between chains.
- F–H · 478 Ų buried · 9 hydrogen bonds · protein-protein
- A–C · 471 Ų buried · 8 hydrogen bonds · protein-protein
- B–J · 469 Ų buried · 7 hydrogen bonds · protein-protein
- D–I · 395 Ų buried · 5 hydrogen bonds · protein-protein
- E–G · 342 Ų buried · 4 hydrogen bonds · protein-protein
Compared structures
- 7AG7 · Crystal structure of SFP aldolase YihT from Salmonella enterica in complex with sulfate… · the same entry in another collection · chain L against L, 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 Q9L7R9
- Elsewhere: RCSB PDB 7AG7 · PDBe 7AG7 · UniProt Q9L7R9
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