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Crystal structure of human HPF1

Analyse Crystal structure of human HPF1 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6M3G
Type: protein
Length: 303 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Histone parylation factor 1
UniProt: Q9NWY4
Pockets: 1 · best druggability 0.30

Structure

x-ray diffraction · 1 distinct chain · 50% helix, 8% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Histone parylation factor 1	protein	303	50% helix, 8% strand	Q9NWY4

Pockets

1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	57	0.30	0.75	15	empty

Compared structures

6M3G · Crystal structure of human HPF1 · the same entry in another collection · chain A against A, TM-score 1.00
Q9NWY4 · AlphaFold monomer V2.0 prediction for histone parylation factor 1 (Q9NWY4) · a predicted model of the same protein · chain A against A, TM-score 1.00

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 Q9NWY4
Elsewhere: RCSB PDB 6M3G · PDBe 6M3G · UniProt Q9NWY4

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