Research workbench
Nature of the inactivation of elastase by N-peptidyl-O- aroyl hydroxylamine as a function of pH
Analyse Nature of the inactivation of elastase by N-peptidyl-O- aroyl hydroxylamine as… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1ELG
- Type
- protein
- Length
- 240 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Porcine pancreatic elastase
- EC
- 3.4.21.36
- UniProt
- P00772
- Ligands
- BAA, CA
- Pockets
- 1 · best druggability 0.54
Structure
x-ray diffraction · 1 distinct chain · 10% helix, 38% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Porcine pancreatic elastase (EC 3.4.21.36) | protein | 240 | 10% helix, 38% strand | P00772 |
Ligands and binding sites
- BAA · (tert-butyloxycarbonyl)-alanyl-alanyl-amine · ligand · chains A
- CA · Calcium ion · metal · chains A
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 | 53 | 0.54 | 0.89 | 18 | empty |
Modifications
Observed in the structure: 4 disulfide, 1 covalent (disulfide, covalent ligand).
Compared structures
- 1ELG · Nature of the inactivation of elastase by N-peptidyl-O-aroyl hydroxylamine as a function… · the same entry in another collection · chain A against A, TM-score 1.00
- P00772 · AlphaFold monomer V2.0 prediction for chymotrypsin-like elastase family member 1 (P00772) · a predicted model of the same protein · 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 P00772
- Elsewhere: RCSB PDB 1ELG · PDBe 1ELG · UniProt P00772
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