Research workbench
Protease E35D-apv
Analyse Protease E35D-apv in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5KR0
- Type
- protein
- Length
- 198 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Protease E35D-apv
- UniProt
- C8BD48
- Ligands
- 478
- Pockets
- 1 · best druggability 0.71
Structure
x-ray diffraction · 1 distinct chain · 7% helix, 58% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Protease E35D-apv | protein | 99 | 7% helix, 58% strand | C8BD48 |
Ligands and binding sites
- 478 · {3-[(4-amino-benzenesulfonyl)-isobutyl-amino]-1-benzyl-2-hydroxy-propyl}-carbamic acid tetrahydro-furan-3-yl ester · ligand · chains A, B
- GOL · Glycerol · additive · chains B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 397 | 0.71 | 0.82 | 41 | 478 |
Interfaces
1 interface between chains.
- A–B · 1861 Ų buried · 34 hydrogen bonds · protein-protein
Compared structures
- 5KR0 · Protease E35D-APV · 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 C8BD48
- Elsewhere: RCSB PDB 5KR0 · PDBe 5KR0 · UniProt C8BD48
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