Research workbench
Crystal structure of peptiligase mutant - L217H/M222P
Analyse Crystal structure of peptiligase mutant - L217H/M222P in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7AM4
- Type
- protein
- Length
- 269 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Subtilisin bpn'
- EC
- 3.4.21.62
- UniProt
- P00782
- Ligands
- SO4
- Pockets
- 1 · best druggability 0.31
Structure
x-ray diffraction · 1 distinct chain · 32% helix, 20% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Subtilisin bpn' (EC 3.4.21.62) | protein | 269 | 32% helix, 20% strand | P00782 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
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 | 63 | 0.31 | 0.75 | 21 | SO4 |
Modifications
Observed in the structure: 1 disulfide, 1 modified (disulfide, oxidation).
Compared structures
- 7AM4 · Crystal structure of Peptiligase mutant - L217H/M222P · 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 P00782
- Elsewhere: RCSB PDB 7AM4 · PDBe 7AM4 · UniProt P00782
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.