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Cobalamin-dependent methionine synthase (1-566) from T. maritima (oxidized, orthorhombic)

Analyse Cobalamin-dependent methionine synthase (1-566) from T. maritima (oxidized… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
1Q7Q
Type
protein
Length
1,117 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
12 · best druggability 0.62

Structure

x-ray diffraction · 2 distinct chains · 46% helix, 13% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A5-methyltetrahydrofolate S-homocysteine methyltransferase (EC 2.1.1.13)protein56546% helix, 13% strandQ9WYA5
B5-methyltetrahydrofolate S-homocysteine methyltransferase (EC 2.1.1.13)protein55245% helix, 13% strandQ9WYA5

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
12460.620.8134empty
22710.610.7936empty
31280.540.8215empty
42460.510.7634empty
51180.490.8017empty

Interfaces

1 interface between chains.

  • A–B · 1078 Ų buried · 0 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 1 disulfide (disulfide).

Compared structures

  • 1Q7Q · Cobalamin-dependent methionine synthase (1-566) from T. maritima (Oxidized, Orthorhombic) · the same entry in another collection · chain A against A, TM-score 1.00

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