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Crystal structure of the phd finger of PHF20

Analyse Crystal structure of the phd finger of PHF20 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5TAB
Type: protein
Length: 53 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Phd finger protein 20
UniProt: Q9BVI0
Ligands: ZN

Structure

x-ray diffraction · 1 distinct chain · 6% helix, 13% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Phd finger protein 20	protein	53	6% helix, 13% strand	Q9BVI0

Ligands and binding sites

ZN · Zinc ion · metal · 2 copies · chains A
GOL · Glycerol · additive · chains A

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

Compared structures

5TAB · Crystal Structure of the PHD Finger of PHF20 · the same entry in another collection · chain A against A, TM-score 1.00
Q9BVI0 · AlphaFold monomer V2.0 prediction for phd finger protein 20 (Q9BVI0) · a predicted model of the same protein · chain A against A, TM-score 0.82

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 Q9BVI0
Elsewhere: RCSB PDB 5TAB · PDBe 5TAB · UniProt Q9BVI0

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