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Crystal structure of the 25KDA subunit of human cleavage factor im with AP4A

Analyse Crystal structure of the 25KDA subunit of human cleavage factor im with AP4A in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3BHO
Type: protein
Length: 203 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Cleavage and polyadenylation specificity factor subunit 5
UniProt: O43809
Ligands: B4P
Pockets: 1 · best druggability 0.67

Structure

x-ray diffraction · 1 distinct chain · 24% helix, 37% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Cleavage and polyadenylation specificity factor subunit 5	protein	203	24% helix, 37% strand	O43809

Ligands and binding sites

B4P · Bis(adenosine)-5'-tetraphosphate · ligand · chains A

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

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	444	0.67	0.79	36	B4P

Compared structures

3BHO · Crystal Structure of the 25kDa Subunit of Human Cleavage factor Im with Ap4A · the same entry in another collection · chain A against A, TM-score 1.00
O43809 · AlphaFold monomer V2.0 prediction for cleavage and polyadenylation specificity factor… · a predicted model of the same protein · chain A against A, TM-score 0.97

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 O43809
Elsewhere: RCSB PDB 3BHO · PDBe 3BHO · UniProt O43809

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