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Crystal structure of ferrous form of the Cl2-Tyr157 human cysteine dioxygenase with both uncrosslinked and crosslinked cofactor
Analyse Crystal structure of ferrous form of the Cl2-Tyr157 human cysteine dioxygenase… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6BPW
- Type
- protein
- Length
- 186 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 2.43
- Source
- Homo sapiens
- Molecule
- Cysteine dioxygenase type 1
- EC
- 1.13.11.20
- UniProt
- Q16878
- Ligands
- FE2, SO4
- Pockets
- 1 · best druggability 0.49
Structure
x-ray diffraction · resolution 2.43 · 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 | Q16878 |
Ligands and binding sites
- FE2 · Fe (II) ion · metal · chains A
- SO4 · Sulfate ion · ion · 3 copies · chains A
- GOL · Glycerol · additive · 6 copies · 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, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 118 | 0.49 | 0.80 | 28 | GOL |
Modifications
Observed in the structure: 1 modified (nonstandard).
Compared structures
- 6BPW · Crystal structure of ferrous form of the CL2-TYR157 human cysteine dioxygenase with both… · the same entry in another collection · chain A against A, TM-score 1.00
- Q16878 · AlphaFold monomer V2.0 prediction for cysteine dioxygenase type 1 (Q16878) · a predicted model of the same protein · chain A against A, TM-score 0.99
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 Q16878
- Elsewhere: RCSB PDB 6BPW · PDBe 6BPW · UniProt Q16878
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