MolNFT v1 · #139434 · protein

Structure of the N-terminal domains of PHF1

5XFN · Phd finger protein 1: “Structure of the N-terminal domains of PHF1”. X-ray diffraction, 1 ligand (ZN), 3 pockets (best druggability 0.67). MolNFT v1 #139434 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 5XFN
Type: protein
Length: 301 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: 3 · best druggability 0.67

Structure

x-ray diffraction · 1 distinct chain · 26% helix, 21% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Phd finger protein 1	protein	301	26% helix, 21% 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

3 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	446	0.67	0.79	47	empty
2	78	0.35	0.76	17	empty
3	54	0.34	0.77	11	empty

Compared structures

5XFN · 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 0.99

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

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