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Structure of the N-terminal domains of PHF1

Analyse Structure of the N-terminal domains of PHF1 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5XFO
Type: protein
Length: 315 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Phd finger protein 1
UniProt: O43189
Ligands: ZN
Pockets: 4 · best druggability 0.69

Structure

x-ray diffraction · 1 distinct chain · 26% helix, 22% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Phd finger protein 1	protein	315	26% helix, 22% strand	O43189

Ligands and binding sites

ZN · Zinc ion · metal · 4 copies · chains A

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

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	502	0.69	0.79	48	empty
2	172	0.44	0.75	28	empty
3	60	0.38	0.80	17	empty
4	51	0.32	0.77	14	empty

Compared structures

5XFO · Structure of the N-terminal domains of PHF1 · the same entry in another collection · chain A against A, TM-score 1.00
O43189 · AlphaFold monomer V2.0 prediction for phd finger protein 1 (O43189) · a predicted model of the same protein · chain A against A, TM-score 0.97

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 O43189
Elsewhere: RCSB PDB 5XFO · PDBe 5XFO · UniProt O43189

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