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Crystal strucrure of putative RNA methyltransferase from bacillus anthracis.

Analyse Crystal strucrure of putative RNA methyltransferase from bacillus anthracis. in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4PZK
Type: protein
Length: 318 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: TRNA (CYTIDINE(34)-2'-O)-methyltransferase
EC: 2.1.1.207
UniProt: Q81YT5
Ligands: SAH
Pockets: 1 · best druggability 0.75

Structure

x-ray diffraction · 1 distinct chain · 35% helix, 21% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	TRNA (CYTIDINE(34)-2'-O)-methyltransferase (EC 2.1.1.207)	protein	159	35% helix, 21% strand	Q81YT5

Ligands and binding sites

SAH · S-adenosyl-L-homocysteine · ligand · 2 copies · chains A, B

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	590	0.75	0.82	82	SAH

Interfaces

1 interface between chains.

A–B · 1646 Å² buried · 29 hydrogen bonds · protein-protein

Compared structures

4PZK · Crystal strucrure of putative RNA methyltransferase from Bacillus anthracis. · 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 Q81YT5
Elsewhere: RCSB PDB 4PZK · PDBe 4PZK · UniProt Q81YT5

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