MolNFT v1 · #90338 · protein
1.85 ångström crystal structure of native hypothetical protein SAOUHSC_02783 from staphylococcus aureus
4EGD · Uncharacterized protein SAOUHSC_02783: “1.85 ångström crystal structure of native hypothetical protein SAOUHSC_02783 from staphylococcus aureus”. X-ray diffraction, 2 ligands (CA, CL), 8 pockets (best druggability 0.60). MolNFT v1…
- PDB
- 4EGD
- Type
- protein
- Length
- 441 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Uncharacterized protein SAOUHSC_02783
- UniProt
- Q2FVD0
- Ligands
- CA, CL
- Pockets
- 8 · best druggability 0.60
Structure
x-ray diffraction · 2 distinct chains · 20% helix, 37% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Uncharacterized protein SAOUHSC_02783 | protein | 221 | 19% helix, 37% strand | Q2FVD0 |
| B | Uncharacterized protein SAOUHSC_02783 | protein | 220 | 20% helix, 38% strand | Q2FVD0 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
8 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 171 | 0.60 | 0.83 | 24 | CA |
| 2 | 111 | 0.46 | 0.79 | 22 | empty |
| 3 | 123 | 0.43 | 0.77 | 17 | empty |
| 4 | 96 | 0.41 | 0.77 | 16 | empty |
| 5 | 116 | 0.38 | 0.74 | 24 | empty |
Interfaces
1 interface between chains.
- A–B · 668 Ų buried · 10 hydrogen bonds · protein-protein
Compared structures
- 4EGD · 1.85 Angstrom crystal structure of native hypothetical protein SAOUHSC_02783 from… · the same entry in another collection · chain A against A, TM-score 1.00
- Q2FVD0 · AlphaFold monomer V2.0 prediction for uncharacterized protein SAOUHSC_02783 (Q2FVD0) · a predicted model of the same protein · chain A against A, TM-score 0.97
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 Q2FVD0
- Elsewhere: RCSB PDB 4EGD · PDBe 4EGD · UniProt Q2FVD0
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