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Structure of C126S mutant of plasmodium falciparum triosephosphate isomerase complexed with pga

Analyse Structure of C126S mutant of plasmodium falciparum triosephosphate isomerase… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3PVF
Type: protein
Length: 246 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Triosephosphate isomerase
EC: 5.3.1.1
UniProt: Q07412
Ligands: PGA
Pockets: 1 · best druggability 0.44

Structure

x-ray diffraction · 1 distinct chain · 44% helix, 16% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Triosephosphate isomerase (EC 5.3.1.1)	protein	246	44% helix, 16% strand	Q07412

Ligands and binding sites

PGA · 2-phosphoglycolic acid · ligand · 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, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	134	0.44	0.76	25	empty

Compared structures

3PVF · Structure of C126S mutant of Plasmodium falciparum triosephosphate isomerase complexed… · the same entry in another collection · chain A against A, TM-score 1.00
Q07412 · AlphaFold monomer V2.0 prediction for triosephosphate isomerase (Q07412) · 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 Q07412
Elsewhere: RCSB PDB 3PVF · PDBe 3PVF · UniProt Q07412

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