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MolNFT v1 · #115512 · protein

Structure of Y. lipolytica TRM9-TRM112 complex, a methyltransferase modifying U34 in the anticodon loop of some trnas

5CM2 · TRNA methyltransferase: “Structure of Y. lipolytica TRM9-TRM112 complex, a methyltransferase modifying U34 in the anticodon loop of…”. X-ray diffraction, 1 ligand (ZN), 3 pockets (best druggability 0.60). MolNFT v1 #115512 on…

PDB
5CM2
Type
protein
Length
308 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
TRNA methyltransferase; TRNA methyltransferase activator subunit
UniProt
Q6C999, Q6C4P5
Ligands
ZN
Pockets
3 · best druggability 0.60

Structure

x-ray diffraction · 2 distinct chains · 27% helix, 32% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
ZTRNA methyltransferaseprotein18422% helix, 40% strandQ6C999
MTRNA methyltransferase activator subunitprotein12435% helix, 22% strandQ6C4P5

Ligands and binding sites

  • ZN · Zinc ion · metal · chains M

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

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
12370.600.8025empty
22040.460.7426empty
3740.390.7816empty

Interfaces

1 interface between chains.

  • Z–M · 1192 Ų buried · 20 hydrogen bonds · protein-protein

Compared structures

  • 5CM2 · Structure of Y. lipolytica Trm9-Trm112 complex, a methyltransferase modifying U34 in the… · the same entry in another collection · chain Z against Z, TM-score 1.00

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