Research workbench

Schistosoma mansoni dihydrofolate reductase

Analyse Schistosoma mansoni dihydrofolate reductase in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3VCO
Type: protein
Length: 183 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Dihydrofolate reductase
EC: 1.5.1.3
UniProt: G4VJD6
Ligands: SO4
Pockets: 2 · best druggability 0.58

Structure

x-ray diffraction · 1 distinct chain · 22% helix, 31% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Dihydrofolate reductase (EC 1.5.1.3)	protein	183	22% helix, 31% strand	G4VJD6

Ligands and binding sites

SO4 · Sulfate ion · ion · 3 copies · chains A

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

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	149	0.58	0.83	35	SO4
2	94	0.36	0.75	16	empty

Compared structures

3VCO · Schistosoma mansoni Dihydrofolate reductase · the same entry in another collection · chain A against A, TM-score 1.00
G4VJD6 · AlphaFold monomer V2.0 prediction for dihydrofolate reductase (G4VJD6) · a predicted model of the same protein · chain A against A, TM-score 0.93

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 G4VJD6
Elsewhere: RCSB PDB 3VCO · PDBe 3VCO · UniProt G4VJD6

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