Research workbench
Crystal structure of ALPHA1-antichymotrypsin variant newbg-III-allo: an allosterically controlled new binding globulin with an unprecedentedly high ligand release efficacy
Analyse Crystal structure of ALPHA1-antichymotrypsin variant newbg-III-allo: an… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6HGM
- Type
- protein
- Length
- 363 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Alpha-1-antichymotrypsin
- UniProt
- P01011
- Ligands
- CA, CL
- Pockets
- 3 · best druggability 0.54
Structure
x-ray diffraction · 2 distinct chains · 31% helix, 38% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Alpha-1-antichymotrypsin | protein | 330 | 34% helix, 37% strand | P01011 |
| B | Alpha-1-antichymotrypsin | protein | 33 | 0% helix, 48% strand | P01011 |
Ligands and binding sites
- CA · Calcium ion · metal · 3 copies · chains A
- CL · Chloride ion · ion · 3 copies · chains A, B
- EDO · 1,2-ethanediol · additive · 2 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 147 | 0.54 | 0.80 | 18 | empty |
| 2 | 52 | 0.46 | 0.84 | 14 | empty |
| 3 | 73 | 0.37 | 0.78 | 15 | empty |
Interfaces
1 interface between chains.
- A–B · 2430 Ų buried · 32 hydrogen bonds · protein-protein
Compared structures
- 6HGM · Crystal structure of Alpha1-antichymotrypsin variant NewBG-III-allo: 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 0.93
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 6HGM · PDBe 6HGM · UniProt P01011
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