Research workbench
Solution structure of staphostatin a form staphylococcus aureus confirms the discovery of a novel class of cysteine proteinase inhibitors.
Analyse Solution structure of staphostatin a form staphylococcus aureus confirms the… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1OH1
- Type
- protein
- Length
- 109 residues
- Chains
- 1
- Method
- solution nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Staphostatin a
- UniProt
- Q99SX7
- Pockets
- 1 · best druggability 0.43
Structure
solution nmr · 1 distinct chain · 6% helix, 40% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Staphostatin a | protein | 109 | 6% helix, 40% strand | Q99SX7 |
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 | 83 | 0.43 | 0.79 | 20 | empty |
Modifications
Observed in the structure: 1 disulfide (disulfide).
Compared structures
- 1OH1 · Solution structure of staphostatin A form Staphylococcus aureus confirms the discovery of… · 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 Q99SX7
- Elsewhere: RCSB PDB 1OH1 · PDBe 1OH1 · UniProt Q99SX7
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