MolNFT v1 · #92379 · protein

Crystal structure of a COG1565 superfamily member and likely methyl transferase from burkholderia thailandensis bound to S-adenosyl- homocysteine

4G67 · Uncharacterized acr, COG1565 superfamily: “Crystal structure of a COG1565 superfamily member and likely methyl transferase from burkholderia…”. X-ray diffraction, 2 ligands (SAH, SO4), 3 pockets (best druggability 0.74). MolNFT v1…

PDB: 4G67
Type: protein
Length: 387 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Uncharacterized acr, COG1565 superfamily
UniProt: Q2T1U7
Ligands: SAH, SO4
Pockets: 3 · best druggability 0.74

Structure

x-ray diffraction · 1 distinct chain · 39% helix, 23% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Uncharacterized acr, COG1565 superfamily	protein	387	39% helix, 23% strand	Q2T1U7

Ligands and binding sites

SAH · S-adenosyl-L-homocysteine · ligand · chains A
SO4 · Sulfate ion · ion · 2 copies · chains A
EDO · 1,2-ethanediol · additive · 2 copies · chains A

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.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	458	0.74	0.83	60	SAH, EDO
2	127	0.41	0.75	23	empty
3	93	0.38	0.76	16	empty

Compared structures

4G67 · Crystal structure of a COG1565 superfamily member and likely methyl transferase from… · 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 Q2T1U7
Elsewhere: RCSB PDB 4G67 · PDBe 4G67 · UniProt Q2T1U7

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