Research workbench
Cysteine dioxygenase variant - C93A at pH 6.2 with cysteine
Analyse Cysteine dioxygenase variant - C93A at pH 6.2 with cysteine in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4XFG
- Type
- protein
- Length
- 186 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Cysteine dioxygenase type 1
- EC
- 1.13.11.20
- UniProt
- P21816
- Ligands
- CYS, FE, CL
- Pockets
- 1 · best druggability 0.53
Structure
x-ray diffraction · 1 distinct chain · 17% helix, 37% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Cysteine dioxygenase type 1 (EC 1.13.11.20) | protein | 186 | 17% helix, 37% strand | P21816 |
Ligands and binding sites
- CYS · Cysteine · ligand · chains A
- FE · Fe (III) ion · metal · chains A
- CL · Chloride ion · ion · chains A
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 | 101 | 0.53 | 0.83 | 28 | CYS, CL |
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 P21816
- Elsewhere: RCSB PDB 4XFG · PDBe 4XFG · UniProt P21816
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