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Crystal structure of putative DNA modification methyltransferase encoded within prophage cp-933R (E.COLI)

Analyse Crystal structure of putative DNA modification methyltransferase encoded within… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3G7U
Type: protein
Length: 348 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Cytosine-specific methyltransferase
EC: 2.1.1.37
UniProt: Q8X8S5
Ligands: CL
Pockets: 5 · best druggability 0.62

Structure

x-ray diffraction · 1 distinct chain · 38% helix, 16% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Cytosine-specific methyltransferase (EC 2.1.1.37)	protein	348	38% helix, 16% strand	Q8X8S5

Ligands and binding sites

CL · Chloride ion · ion · chains A
GOL · Glycerol · additive · 2 copies · chains A

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

Pockets

5 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	367	0.62	0.78	47	empty
2	74	0.50	0.83	15	GOL
3	106	0.40	0.76	19	empty
4	52	0.36	0.79	15	empty
5	72	0.32	0.74	14	empty

Compared structures

3G7U · Crystal structure of putative DNA modification methyltransferase encoded within prophage… · 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 Q8X8S5
Elsewhere: RCSB PDB 3G7U · PDBe 3G7U · UniProt Q8X8S5

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