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Crystal structure of trml from mycoplasma capricolum

Analyse Crystal structure of trml from mycoplasma capricolum in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 7E3T
Type: protein
Length: 174 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Putative tRNA (CYTIDINE(34)-2'-O)-methyltransferase
EC: 2.1.1.207
UniProt: A0A0C2ZKK6
Pockets: 1 · best druggability 0.52

Structure

x-ray diffraction · 1 distinct chain · 36% helix, 20% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Putative tRNA (CYTIDINE(34)-2'-O)-methyltransferase (EC 2.1.1.207)	protein	174	36% helix, 20% strand	A0A0C2ZKK6

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	172	0.52	0.79	24	empty

Compared structures

7E3T · Crystal structure of TrmL from Mycoplasma capricolum · 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 A0A0C2ZKK6
Elsewhere: RCSB PDB 7E3T · PDBe 7E3T · UniProt A0A0C2ZKK6

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