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Cobalamin-dependent methionine synthase (meth) from thermotoga maritima (oxidized, monoclinic)

Analyse Cobalamin-dependent methionine synthase (meth) from thermotoga maritima… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
1Q7M
Type
protein
Length
1,107 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
5-methyltetrahydrofolate S-homocysteine methyltransferase
EC
2.1.1.13
UniProt
Q9WYA5
Pockets
7 · best druggability 0.64

Structure

x-ray diffraction · 2 distinct chains · 47% helix, 14% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A5-methyltetrahydrofolate S-homocysteine methyltransferase (EC 2.1.1.13)protein55947% helix, 15% strandQ9WYA5
B5-methyltetrahydrofolate S-homocysteine methyltransferase (EC 2.1.1.13)protein54847% helix, 13% strandQ9WYA5

Pockets

7 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
13040.640.8037empty
23040.620.7945empty
33370.580.7737empty
42580.500.7530empty
51310.490.7923empty

Interfaces

1 interface between chains.

  • A–B · 1103 Ų buried · 1 hydrogen bond · protein-protein

Modifications

Observed in the structure: 2 disulfide (disulfide).

Compared structures

  • 1Q7M · Cobalamin-dependent methionine synthase (MetH) from Thermotoga maritima (Oxidized… · the same entry in another collection · chain A against A, TM-score 1.00

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