MolNFT v1 · #69501 · protein
Structure of frmsr of staphylococcus aureus (reduced form)
3KSF · Putative uncharacterized protein: “Structure of frmsr of staphylococcus aureus (reduced form)”. X-ray diffraction, 9 pockets (best druggability 0.69). MolNFT v1 #69501 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 3KSF
- Type
- protein
- Length
- 1,220 residues
- Chains
- 8
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Putative uncharacterized protein
- EC
- 1.8.4.14
- UniProt
- Q6GFY9
- Pockets
- 9 · best druggability 0.69
Structure
x-ray diffraction · 2 distinct chains · 37% helix, 27% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, E, F, G | Putative uncharacterized protein (EC 1.8.4.14) | protein | 152 | 37% helix, 27% strand | Q6GFY9 |
| D, H | Putative uncharacterized protein (EC 1.8.4.14) | protein | 154 | 37% helix, 27% strand | Q6GFY9 |
Ligands and binding sites
- PEG · Di(hydroxyethyl)ether · additive · chains C, D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
9 pockets found on a 1 Å grid, 7 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 341 | 0.69 | 0.82 | 43 | empty |
| 2 | 416 | 0.66 | 0.79 | 46 | empty |
| 3 | 132 | 0.64 | 0.87 | 24 | empty |
| 4 | 230 | 0.63 | 0.82 | 28 | empty |
| 5 | 190 | 0.62 | 0.83 | 29 | empty |
Interfaces
6 interfaces between chains.
- G–H · 953 Ų buried · 15 hydrogen bonds · protein-protein
- C–D · 948 Ų buried · 15 hydrogen bonds · protein-protein
- A–B · 946 Ų buried · 18 hydrogen bonds · protein-protein
- E–F · 941 Ų buried · 15 hydrogen bonds · protein-protein
- D–G · 243 Ų buried · 3 hydrogen bonds · protein-protein
Compared structures
- 3KSF · structure of fRMsr of Staphylococcus aureus (reduced form) · 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 Q6GFY9
- Elsewhere: RCSB PDB 3KSF · PDBe 3KSF · UniProt Q6GFY9
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