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Methyltransferase from methanosarcina mazei

Analyse Methyltransferase from methanosarcina mazei in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4AY7
Type: protein
Length: 674 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Methylcobalamin\: coenzyme M methyltransferase
EC: 2.1.1.247
UniProt: Q8PXZ6
Ligands: ZN, MG
Pockets: 3 · best druggability 0.61

Structure

x-ray diffraction · 1 distinct chain · 51% helix, 12% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Methylcobalamin\: coenzyme M methyltransferase (EC 2.1.1.247)	protein	337	51% helix, 12% strand	Q8PXZ6

Ligands and binding sites

ZN · Zinc ion · metal · 2 copies · chains A, B
MG · Magnesium ion · metal · 2 copies · chains A, B

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

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	505	0.61	0.75	54	empty
2	208	0.51	0.76	36	empty
3	187	0.49	0.76	31	empty

Interfaces

1 interface between chains.

A–B · 255 Å² buried · 5 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 2 modified (oxidation).

Compared structures

4AY7 · methyltransferase from Methanosarcina mazei · 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 Q8PXZ6
Elsewhere: RCSB PDB 4AY7 · PDBe 4AY7 · UniProt Q8PXZ6

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