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PHF23 phd domain apo

Analyse PHF23 phd domain apo in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
6WXK
Type
protein
Length
248 residues
Chains
5
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Phd finger protein 23
UniProt
Q9BUL5
Ligands
ZN
Pockets
2 · best druggability 0.54

Structure

x-ray diffraction · 4 distinct chains · 2% helix, 17% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
APhd finger protein 23protein490% helix, 12% strandQ9BUL5
B, CPhd finger protein 23protein518% helix, 16% strandQ9BUL5
DPhd finger protein 23protein500% helix, 22% strandQ9BUL5
EPhd finger protein 23protein470% helix, 17% strandQ9BUL5

Ligands and binding sites

  • ZN · Zinc ion · metal · 10 copies · chains A, B, C, D, E

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
11740.540.7929empty
21380.450.7720empty

Interfaces

6 interfaces between chains.

  • B–C · 584 Ų buried · 10 hydrogen bonds · protein-protein
  • A–B · 572 Ų buried · 7 hydrogen bonds · protein-protein
  • C–D · 564 Ų buried · 12 hydrogen bonds · protein-protein
  • A–C · 67 Ų buried · 0 hydrogen bonds · protein-protein
  • B–D · 39 Ų buried · 0 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 2 disulfide (disulfide).

Compared structures

  • 6WXK · PHF23 PHD Domain Apo · the same entry in another collection · chain E against E, TM-score 1.00
  • Q9BUL5 · AlphaFold monomer V2.0 prediction for phd finger protein 23 (Q9BUL5) · a predicted model of the same protein · chain A against A, TM-score 0.92

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