MolNFT v1 · #27122 · protein
Crystal structure of the human BETA2-chimaerin
1XA6: “Crystal structure of the human BETA2-chimaerin”. X-ray diffraction, 1 ligand (ZN), 4 pockets (best druggability 0.73). MolNFT v1 #27122 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 1XA6
- Type
- protein
- Length
- 399 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- BETA2-chimaerin
- UniProt
- P52757
- Ligands
- ZN
- Pockets
- 4 · best druggability 0.73
Structure
x-ray diffraction · 1 distinct chain · 36% helix, 8% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | BETA2-chimaerin | protein | 399 | 36% helix, 8% strand | P52757 |
Ligands and binding sites
- ZN · Zinc ion · metal · 2 copies · 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, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 584 | 0.73 | 0.80 | 78 | empty |
| 2 | 58 | 0.54 | 0.88 | 16 | empty |
| 3 | 160 | 0.47 | 0.77 | 23 | empty |
| 4 | 99 | 0.38 | 0.75 | 21 | 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 P52757
- Elsewhere: RCSB PDB 1XA6 · PDBe 1XA6 · UniProt P52757
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