Research workbench
Crystal structure of Alpha1-antichymotrypsin variant DBS-I-allo1: an allosterically triggered drug-binding serpin for doxycycline
Analyse Crystal structure of Alpha1-antichymotrypsin variant DBS-I-allo1: an… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5OM5
- Type
- protein
- Length
- 372 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 1.595
- Source
- Homo sapiens
- Molecule
- Alpha-1-antichymotrypsin
- UniProt
- P01011
- Ligands
- CL
- Pockets
- 4 · best druggability 0.60
Structure
x-ray diffraction · resolution 1.595 · 2 distinct chains · 31% helix, 37% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Alpha-1-antichymotrypsin | protein | 338 | 34% helix, 36% strand | P01011 |
| B | Alpha-1-antichymotrypsin | protein | 34 | 0% helix, 47% strand | P01011 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
4 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 95 | 0.60 | 0.87 | 26 | empty |
| 2 | 94 | 0.38 | 0.76 | 19 | empty |
| 3 | 64 | 0.31 | 0.75 | 13 | empty |
| 4 | 56 | 0.25 | 0.73 | 17 | empty |
Interfaces
1 interface between chains.
- A–B · 2555 Ų buried · 36 hydrogen bonds · protein-protein
Compared structures
- 5OM5 · Crystal structure of ALPHA1-antichymotrypsin variant dbs-I-ALLO1: an allosterically… · the same entry in another collection · chain A against A, TM-score 1.00
- P01011 · AlphaFold monomer V2.0 prediction for alpha-1-antichymotrypsin (P01011) · a predicted model of the same protein · chain A against A, TM-score 0.92
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 P01011
- Elsewhere: RCSB PDB 5OM5 · PDBe 5OM5 · UniProt P01011
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