MolNFT v1 · #144311 · protein
Crystal structure of cysteine, nitric oxide-bound ferrous form of the uncrosslinked F2-TYR157 human cysteine dioxygenase
6BPR · Cysteine dioxygenase type 1: “Crystal structure of cysteine, nitric oxide-bound ferrous form of the uncrosslinked F2-TYR157 human cysteine…”. X-ray diffraction, 4 ligands (CYS, FE, SO4), 1 pocket (best druggability 0.55). MolNFT v1…
- PDB
- 6BPR
- 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
- Q16878
- Ligands
- CYS, FE, SO4, NO
- Pockets
- 1 · best druggability 0.55
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 | Q16878 |
Ligands and binding sites
- CYS · Cysteine · ligand · chains A
- FE · Fe (III) ion · metal · chains A
- SO4 · Sulfate ion · ion · 3 copies · chains A
- NO · Nitric oxide · ion · chains A
- GOL · Glycerol · additive · 7 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 | 102 | 0.55 | 0.84 | 26 | FE, CYS, NO, GOL |
Modifications
Observed in the structure: 1 modified (nonstandard).
Compared structures
- 6BPR · Crystal structure of cysteine, nitric oxide-bound ferrous form of the uncrosslinked… · 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 6BPR · PDBe 6BPR · UniProt Q16878
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