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Structure of a O-methyltransferase from mycobacterium tuberculosis at 2.0 resolution

Analyse Structure of a O-methyltransferase from mycobacterium tuberculosis at 2.0… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5X7F
Type: protein
Length: 198 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Putative O-methyltransferase RV1220C
EC: 2.1.1.-
UniProt: P9WJZ7
Ligands: SAM
Pockets: 1 · best druggability 0.48

Structure

x-ray diffraction · 1 distinct chain · 46% helix, 22% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Putative O-methyltransferase RV1220C (EC 2.1.1.-)	protein	198	46% helix, 22% strand	P9WJZ7

Ligands and binding sites

SAM · S-adenosylmethionine · 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, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	157	0.48	0.77	30	SAM

Compared structures

5X7F · Structure of a O-methyltransferase from Mycobacterium tuberculosis at 2.0 resolution · the same entry in another collection · chain A against A, TM-score 1.00
P9WJZ7 · AlphaFold monomer V2.0 prediction for putative O-methyltransferase RV1220C (P9WJZ7) · a predicted model of the same protein · chain A against A, TM-score 0.99

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 P9WJZ7
Elsewhere: RCSB PDB 5X7F · PDBe 5X7F · UniProt P9WJZ7

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