MolNFT v1 · #161424 · protein

Structure of M. capricolum trmk in complex with the natural cofactor product S-adenosyl-homocysteine (sah)

6QE6 · TRNA (ADENINE(22)-N(1))-methyltransferase: “Structure of M. capricolum trmk in complex with the natural cofactor product S-adenosyl-homocysteine (sah)”. X-ray diffraction, 1 ligand (SAH), 2 pockets (best druggability 0.35). MolNFT…

PDB: 6QE6
Type: protein
Length: 452 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: TRNA (ADENINE(22)-N(1))-methyltransferase
EC: 2.1.1.217
UniProt: A0A0C3A3T0
Ligands: SAH
Pockets: 2 · best druggability 0.35

Structure

x-ray diffraction · 1 distinct chain · 43% helix, 23% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	TRNA (ADENINE(22)-N(1))-methyltransferase (EC 2.1.1.217)	protein	226	43% helix, 23% strand	A0A0C3A3T0

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

2 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	70	0.35	0.77	17	empty
2	52	0.32	0.77	16	empty

Interfaces

1 interface between chains.

A–B · 418 Å² buried · 8 hydrogen bonds · protein-protein

Compared structures

6QE6 · Structure of M. capricolum TrmK in complex with the natural cofactor product… · the same entry in another collection · chain B against B, 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 A0A0C3A3T0
Elsewhere: RCSB PDB 6QE6 · PDBe 6QE6 · UniProt A0A0C3A3T0

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