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Structural basis for UTP specificity of RNA editing tutases from trypanosoma brucei

Analyse Structural basis for UTP specificity of RNA editing tutases from trypanosoma… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2B51
Type: protein
Length: 444 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: RNA editing complex protein MP57
UniProt: Q86MV5
Ligands: UTP, MN
Pockets: 1 · best druggability 0.73

Structure

x-ray diffraction · 1 distinct chain · 46% helix, 14% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	RNA editing complex protein MP57	protein	444	46% helix, 14% strand	Q86MV5

Ligands and binding sites

UTP · Uridine 5'-triphosphate · ligand · 3 copies · chains A
MN · Manganese (II) ion · metal · 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	669	0.73	0.79	50	MN, UTP

Compared structures

2B51 · Structural Basis for UTP Specificity of RNA Editing TUTases from Trypanosoma Brucei · the same entry in another collection · chain A against A, TM-score 1.00
Q86MV5 · AlphaFold monomer V2.0 prediction for terminal uridylyltransferase 2 (Q86MV5) · 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 Q86MV5
Elsewhere: RCSB PDB 2B51 · PDBe 2B51 · UniProt Q86MV5

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