MolNFT v2 · #129907 · protein
Crystal structure of Alpha1-antichymotrypsin variant DBS-I-allo1: an allosterically triggered drug-binding serpin for doxycycline
5OM5: “Crystal structure of Alpha1-antichymotrypsin variant DBS-I-allo1: an allosterically triggered drug-binding…”. X-ray diffraction at 1.595, 1 ligand (CL). MolNFT v2 #129907 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- 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
- UniProt
- P01011
- Ligands
- CL
Structure
x-ray diffraction · resolution 1.595 · 2 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 338 | — | P01011 |
| B | — | protein | 34 | — | P01011 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
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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