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Crystal structure of the 25 kda subunit of human cleavage factor im

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

PDB: 3BAP
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
Pockets: 1 · best druggability 0.68

Structure

x-ray diffraction · 1 distinct chain · 24% helix, 35% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Cleavage and polyadenylation specificity factor subunit 5	protein	203	24% helix, 35% strand	O43809

Ligands and binding sites

GOL · Glycerol · additive · 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	419	0.68	0.80	39	GOL

Modifications

Observed in the structure: 3 modified (engineered).

Compared structures

3BAP · Crystal Structure of the 25 kDa Subunit of Human Cleavage Factor Im · 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 0.98

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

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