Research workbench
The crystal structure of nickel bound human ado C18S C239S variant
Analyse The crystal structure of nickel bound human ado C18S C239S variant in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7REI
- Type
- protein
- Length
- 243 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- 2-aminoethanethiol dioxygenase
- EC
- 1.13.11.19
- UniProt
- Q96SZ5
- Ligands
- NI
- Pockets
- 1 · best druggability 0.55
Structure
x-ray diffraction · 1 distinct chain · 18% helix, 37% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | 2-aminoethanethiol dioxygenase (EC 1.13.11.19) | protein | 243 | 18% helix, 37% strand | Q96SZ5 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 210 | 0.55 | 0.78 | 28 | NI, GOL |
Compared structures
- 7REI · The crystal structure of nickel bound human ADO C18S C239S variant · the same entry in another collection · chain A against A, TM-score 1.00
- Q96SZ5 · AlphaFold monomer V2.0 prediction for 2-aminoethanethiol dioxygenase (Q96SZ5) · a predicted model of the same protein · chain A against A, TM-score 0.94
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 Q96SZ5
- Elsewhere: RCSB PDB 7REI · PDBe 7REI · UniProt Q96SZ5
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