MolNFT v1 · #10691 · protein
Interactions causing the kinetic trap in serpin protein folding
1IZ2 · ALPHA1-antitrypsin: “Interactions causing the kinetic trap in serpin protein folding”. X-ray diffraction, 2 ligands (Z6W, GLC), 4 pockets (best druggability 0.57). MolNFT v1 #10691 on GenesisL1: 3D structure, binding sites and…
- PDB
- 1IZ2
- Type
- protein
- Length
- 371 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- ALPHA1-antitrypsin
- UniProt
- P01009
- Ligands
- Z6W, GLC
- Pockets
- 4 · best druggability 0.57
Structure
x-ray diffraction · 1 distinct chain · 28% helix, 33% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | ALPHA1-antitrypsin | protein | 371 | 28% helix, 33% strand | P01009 |
Ligands and binding sites
- Z6W · (5R)-5-[(2R)-2-hydroxynonyl]-beta-D-xylulofuranose · ligand · chains A
- GLC · alpha-D-glucopyranose · sugar · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
4 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 192 | 0.57 | 0.79 | 23 | Z6W |
| 2 | 101 | 0.55 | 0.84 | 23 | empty |
| 3 | 109 | 0.54 | 0.82 | 17 | empty |
| 4 | 136 | 0.46 | 0.77 | 25 | empty |
Compared structures
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 P01009
- Elsewhere: RCSB PDB 1IZ2 · PDBe 1IZ2 · UniProt P01009
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