Research workbench
1510-N membrane-bound stomatin-specific protease S97A mutant
Analyse 1510-N membrane-bound stomatin-specific protease S97A mutant in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6M4B
- Type
- protein
- Length
- 414 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 2.25
- Source
- Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139…
- Molecule
- Membrane-bound protease PH1510
- EC
- 3.4.21.-
- UniProt
- O59179
- Ligands
- SO4
- Pockets
- 3 · best druggability 0.69
Structure
x-ray diffraction · resolution 2.25 · 1 distinct chain · 36% helix, 25% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Membrane-bound protease PH1510 (EC 3.4.21.-) | protein | 207 | 36% helix, 25% strand | O59179 |
Ligands and binding sites
- SO4 · Sulfate ion · ion · 2 copies · chains B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 55 | 0.69 | 0.97 | 18 | empty |
| 2 | 376 | 0.62 | 0.77 | 48 | empty |
| 3 | 253 | 0.61 | 0.80 | 27 | empty |
Interfaces
1 interface between chains.
- A–B · 941 Ų buried · 13 hydrogen bonds · protein-protein
Compared structures
- 6M4B · 1510-N membrane-bound stomatin-specific protease S97A mutant · the same entry in another collection · chain A against A, TM-score 1.00
- O59179 · AlphaFold monomer V2.0 prediction for membrane-bound protease PH1510 (O59179) · a predicted model of the same protein · chain A against A, TM-score 0.99
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 O59179
- Elsewhere: RCSB PDB 6M4B · PDBe 6M4B · UniProt O59179
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