Research workbench

Structure of human cpsf-73

Analyse Structure of human cpsf-73 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2I7T
Type: protein
Length: 404 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Cleavage and polyadenylation specificity factor 73 kda subunit
UniProt: Q9UKF6
Ligands: ZN, SO4
Pockets: 3 · best druggability 0.76

Structure

x-ray diffraction · 1 distinct chain · 30% helix, 25% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Cleavage and polyadenylation specificity factor 73 kda subunit	protein	404	30% helix, 25% strand	Q9UKF6

Ligands and binding sites

ZN · Zinc ion · metal · 2 copies · chains A
SO4 · Sulfate ion · ion · 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	428	0.76	0.85	55	SO4
2	167	0.47	0.76	22	empty
3	93	0.37	0.76	19	empty

Compared structures

2I7T · Structure of human CPSF-73 · the same entry in another collection · chain A against A, TM-score 1.00
Q9UKF6 · AlphaFold monomer V2.0 prediction for cleavage and polyadenylation specificity factor… · a predicted model of the same protein · chain A against A, TM-score 0.98

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 Q9UKF6
Elsewhere: RCSB PDB 2I7T · PDBe 2I7T · UniProt Q9UKF6

GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.