MolNFT v1 · #39921 · protein
Structural genomics, the crystal structure of full-length spovg from staphylococcus epidermidis atcc 12228
2I9Z · Putative septation protein spovg: “Structural genomics, the crystal structure of full-length spovg from staphylococcus epidermidis atcc 12228”. X-ray diffraction, 1 pocket (best druggability 0.31). MolNFT v1 #39921 on GenesisL1: 3D…
- PDB
- 2I9Z
- Type
- protein
- Length
- 171 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Putative septation protein spovg
- UniProt
- Q8CML1
- Pockets
- 1 · best druggability 0.31
Structure
x-ray diffraction · 2 distinct chains · 19% helix, 47% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Putative septation protein spovg | protein | 87 | 18% helix, 48% strand | Q8CML1 |
| B | Putative septation protein spovg | protein | 84 | 20% helix, 45% strand | Q8CML1 |
Ligands and binding sites
- EDO · 1,2-ethanediol · additive · 4 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 81 | 0.31 | 0.73 | 14 | EDO |
Interfaces
1 interface between chains.
- A–B · 1047 Ų buried · 13 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 10 modified (engineered).
Compared structures
- 2I9Z · Structural Genomics, the Crystal structure of full-length SpoVG from Staphylococcus… · the same entry in another collection · chain A against A, TM-score 1.00
- Q8CML1 · AlphaFold monomer V2.0 prediction for putative septation protein spovg (Q8CML1) · a predicted model of the same protein · chain B against A, TM-score 0.95
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 Q8CML1
- Elsewhere: RCSB PDB 2I9Z · PDBe 2I9Z · UniProt Q8CML1
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