Research workbench
Crystal structure of PH0851
Analyse Crystal structure of PH0851 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2YXL
- Type
- protein
- Length
- 443 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- 450AA long hypothetical fmu protein
- UniProt
- O58581
- Ligands
- SFG
- Pockets
- 2 · best druggability 0.83
Structure
x-ray diffraction · 1 distinct chain · 50% helix, 14% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | 450AA long hypothetical fmu protein | protein | 443 | 50% helix, 14% strand | O58581 |
Ligands and binding sites
- SFG · Sinefungin · ligand · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1127 | 0.83 | 0.83 | 99 | SFG |
| 2 | 92 | 0.36 | 0.75 | 22 | empty |
Compared structures
- 2YXL · Crystal Structure of PH0851 · 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 O58581
- Elsewhere: RCSB PDB 2YXL · PDBe 2YXL · UniProt O58581
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