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Crystal structure of ferrous form of the uncrosslinked F2-TYR157 human cysteine dioxygenase

Analyse Crystal structure of ferrous form of the uncrosslinked F2-TYR157 human cysteine… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
6BPT
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
FE2, SO4
Pockets
1 · best druggability 0.50

Structure

x-ray diffraction · 1 distinct chain · 17% helix, 37% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
ACysteine dioxygenase type 1 (EC 1.13.11.20)protein18617% helix, 37% strandQ16878

Ligands and binding sites

  • FE2 · Fe (II) ion · metal · chains A
  • SO4 · Sulfate ion · ion · 4 copies · chains A
  • GOL · Glycerol · additive · 3 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.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
11160.500.8129SO4

Modifications

Observed in the structure: 1 modified (nonstandard).

Compared structures

  • 6BPT · Crystal structure of ferrous form of the uncrosslinked F2-Tyr157 human cysteine… · 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

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