Research workbench
Fmdv leader protease (lbshort-C51A-C133S)
Analyse Fmdv leader protease (lbshort-C51A-C133S) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1QMY
- Type
- protein
- Length
- 468 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Protease
- UniProt
- P03305
- Pockets
- 2 · best druggability 0.57
Structure
x-ray diffraction · 1 distinct chain · 29% helix, 26% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C | Protease | protein | 156 | 29% helix, 26% strand | P03305 |
Ligands and binding sites
- EDO · 1,2-ethanediol · additive · 2 copies · chains B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 265 | 0.57 | 0.78 | 32 | empty |
| 2 | 143 | 0.50 | 0.79 | 27 | empty |
Interfaces
2 interfaces between chains.
- A–B · 495 Ų buried · 10 hydrogen bonds · protein-protein
- B–C · 114 Ų buried · 0 hydrogen bonds · protein-protein
Compared structures
- 1QMY · Fmdv leader protease (lbshort-C51A-C133S) · 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 P03305
- Elsewhere: RCSB PDB 1QMY · PDBe 1QMY · UniProt P03305
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