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Crystal structure of human BRR2 in complex with T-3935799

Analyse Crystal structure of human BRR2 in complex with T-3935799 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5URK
Type: protein
Length: 1,706 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: U5 small nuclear ribonucleoprotein 200 kda helicase
EC: 3.6.4.13
UniProt: O75643
Ligands: 8LP
Pockets: 16 · best druggability 0.80

Structure

x-ray diffraction · 1 distinct chain · 43% helix, 17% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	U5 small nuclear ribonucleoprotein 200 kda helicase (EC 3.6.4.13)	protein	1706	43% helix, 17% strand	O75643

Ligands and binding sites

8LP · 6-benzyl-3-[3-(benzyloxy)phenyl]-4,6-dihydropyrido[4,3-d]pyrimidine-2,7(1H,3H)-dione · ligand · chains A
GOL · Glycerol · additive · chains A

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

Pockets

16 pockets found on a 1 Å grid, 10 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	460	0.80	0.87	57	GOL, 8LP
2	995	0.80	0.81	100	empty
3	967	0.79	0.81	85	empty
4	446	0.79	0.87	61	empty
5	737	0.74	0.80	48	empty

Compared structures

5URK · Crystal structure of human BRR2 in complex with T-3935799 · the same entry in another collection · 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 O75643
Elsewhere: RCSB PDB 5URK · PDBe 5URK · UniProt O75643

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