MolNFT v1 · #15054 · protein

Methionine synthase (activation domain)

1MSK · Cobalamin-dependent methionine synthase: “Methionine synthase (activation domain)”. X-ray diffraction, 1 ligand (SAM), 1 pocket (best druggability 0.53). MolNFT v1 #15054 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 1MSK
Type: protein
Length: 327 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Cobalamin-dependent methionine synthase
EC: 2.1.1.13
UniProt: P13009
Ligands: SAM
Pockets: 1 · best druggability 0.53

Structure

x-ray diffraction · 1 distinct chain · 41% helix, 17% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Cobalamin-dependent methionine synthase (EC 2.1.1.13)	protein	327	41% helix, 17% strand	P13009

Ligands and binding sites

SAM · S-adenosylmethionine · ligand · chains A
ACT · Acetate ion · additive · chains A

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

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	217	0.53	0.77	36	SAM

Compared structures

1MSK · Methionine synthase (activation domain) · the same entry in another collection · chain A against A, TM-score 1.00
P13009 · AlphaFold monomer V2.0 prediction for methionine synthase (P13009) · a predicted model of the same protein · chain A against A, TM-score 0.99

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 P13009
Elsewhere: RCSB PDB 1MSK · PDBe 1MSK · UniProt P13009

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