MolNFT v1 · #137442 · protein

Methionine synthase folate-binding domain from thermus thermophilus HB8

5VON · 5-methyltetrahydrofolate homocysteine S-methyltransferase: “Methionine synthase folate-binding domain from thermus thermophilus HB8”. X-ray diffraction, 1 pocket (best druggability 0.64). MolNFT v1 #137442 on GenesisL1: 3D…

PDB: 5VON
Type: protein
Length: 282 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: 5-methyltetrahydrofolate homocysteine S-methyltransferase
UniProt: Q5SKM5
Pockets: 1 · best druggability 0.64

Structure

x-ray diffraction · 1 distinct chain · 51% helix, 17% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	5-methyltetrahydrofolate homocysteine S-methyltransferase	protein	282	51% helix, 17% strand	Q5SKM5

Ligands and binding sites

GOL · Glycerol · 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	477	0.64	0.77	51	empty

Compared structures

5VON · Methionine synthase folate-binding domain from Thermus thermophilus HB8 · 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 Q5SKM5
Elsewhere: RCSB PDB 5VON · PDBe 5VON · UniProt Q5SKM5

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