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 v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P01011
- Ligands
- CL
Structure
x-ray diffraction · 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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