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Crystal structure of TFB1M and H45 in homo sapiens

Analyse Crystal structure of TFB1M and H45 in homo sapiens in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6AJK
Type: protein + RNA
Length: 321 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Dimethyladenosine transferase 1, mitochondrial; RNA (28-mer)
EC: 2.1.1.-
UniProt: Q8WVM0
Pockets: 3 · best druggability 0.64

Structure

x-ray diffraction · 2 distinct chains · 43% helix, 16% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Dimethyladenosine transferase 1, mitochondrial (EC 2.1.1.-)	protein	293	43% helix, 16% strand	Q8WVM0
B	RNA (28-mer)	rna	28	—	—

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	125	0.64	0.87	27	empty
2	437	0.56	0.74	28	empty
3	90	0.35	0.75	18	empty

Interfaces

1 interface between chains.

A–B · 952 Å² buried · 21 hydrogen bonds · protein-nucleic

Compared structures

6AJK · Crystal structure of TFB1M and h45 in homo sapiens · the same entry in another collection · chain A against A, TM-score 1.00
Q8WVM0 · AlphaFold monomer V2.0 prediction for dimethyladenosine transferase 1, mitochondrial… · 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 Q8WVM0
Elsewhere: RCSB PDB 6AJK · PDBe 6AJK · UniProt Q8WVM0

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