MolNFT v1 · #22400 · protein

Crystal structure analysis of E.COLI protein (N5)-glutamine methyltransferase (hemk)

1T43 · Protein methyltransferase hemk: “Crystal structure analysis of E.COLI protein (N5)-glutamine methyltransferase (hemk)”. X-ray diffraction, 1 ligand (SAH), 2 pockets (best druggability 0.73). MolNFT v1 #22400 on GenesisL1: 3D…

PDB: 1T43
Type: protein
Length: 274 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Protein methyltransferase hemk
EC: 2.1.1.-
UniProt: P0ACC1
Ligands: SAH
Pockets: 2 · best druggability 0.73

Structure

x-ray diffraction · 1 distinct chain · 40% helix, 15% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Protein methyltransferase hemk (EC 2.1.1.-)	protein	274	40% helix, 15% strand	P0ACC1

Ligands and binding sites

SAH · S-adenosyl-L-homocysteine · ligand · chains A

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

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	376	0.73	0.84	55	SAH
2	187	0.50	0.77	23	empty

Compared structures

1T43 · Crystal Structure Analysis of E.coli Protein (N5)-Glutamine Methyltransferase (HemK) · the same entry in another collection · chain A against A, TM-score 1.00
P0ACC1 · AlphaFold monomer V2.0 prediction for release factor glutamine methyltransferase (P0ACC1) · a predicted model of the same protein · chain A against A, TM-score 0.97

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 P0ACC1
Elsewhere: RCSB PDB 1T43 · PDBe 1T43 · UniProt P0ACC1

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