MolNFT v1 · #144011 · protein
Crystal structure of ferrous form of the crosslinked human cysteine dioxygenase
6BGM · Cysteine dioxygenase type 1: “Crystal structure of ferrous form of the crosslinked human cysteine dioxygenase”. X-ray diffraction, 2 ligands (FE2, SO4), 1 pocket (best druggability 0.53). MolNFT v1 #144011 on GenesisL1: 3D…
- PDB
- 6BGM
- Type
- protein
- Length
- 187 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
- Q16878
- Ligands
- FE2, SO4
- Pockets
- 1 · best druggability 0.53
Structure
x-ray diffraction · 1 distinct chain · 17% helix, 36% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Cysteine dioxygenase type 1 (EC 1.13.11.20) | protein | 187 | 17% helix, 36% strand | Q16878 |
Ligands and binding sites
- FE2 · Fe (II) ion · metal · chains A
- SO4 · Sulfate ion · ion · 3 copies · chains A
- GOL · Glycerol · additive · 2 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, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 164 | 0.53 | 0.79 | 32 | FE2 |
Compared structures
- 6BGM · Crystal structure of ferrous form of the crosslinked human cysteine dioxygenase · 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 6BGM · PDBe 6BGM · UniProt Q16878
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