MolNFT v1 · #35081 · protein

Crystal structure of cbil, a methyltransferase involved in anaerobic vitamin B12 biosynthesis

2E0K · Precorrin-2 C20-methyltransferase: “Crystal structure of cbil, a methyltransferase involved in anaerobic vitamin B12 biosynthesis”. X-ray diffraction, 4 pockets (best druggability 0.79). MolNFT v1 #35081 on GenesisL1: 3D structure…

PDB: 2E0K
Type: protein
Length: 485 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Precorrin-2 C20-methyltransferase
EC: 2.1.1.130
UniProt: Q8KFD9
Pockets: 4 · best druggability 0.79

Structure

x-ray diffraction · 2 distinct chains · 34% helix, 24% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Precorrin-2 C20-methyltransferase (EC 2.1.1.130)	protein	241	33% helix, 24% strand	Q8KFD9
B	Precorrin-2 C20-methyltransferase (EC 2.1.1.130)	protein	244	35% helix, 24% strand	Q8KFD9

Pockets

4 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	393	0.79	0.88	59	empty
2	649	0.77	0.83	70	empty
3	72	0.36	0.77	22	empty
4	60	0.32	0.76	14	empty

Interfaces

1 interface between chains.

A–B · 1967 Å² buried · 30 hydrogen bonds · protein-protein

Compared structures

2E0K · Crystal structure of CbiL, a methyltransferase involved in anaerobic vitamin B12… · 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 Q8KFD9
Elsewhere: RCSB PDB 2E0K · PDBe 2E0K · UniProt Q8KFD9

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