Research workbench

Crystal structure of PFAL009167 a putative D-ribulose 5-phosphate 3- epimerase from P.FALCIPARUM

Analyse Crystal structure of PFAL009167 a putative D-ribulose 5-phosphate 3- epimerase… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1TQX
Type: protein
Length: 442 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: D-ribulose-5-phosphate 3-epimerase, putative
UniProt: Q8I5L3
Ligands: ZN, SO4
Pockets: 2 · best druggability 0.62

Structure

x-ray diffraction · 1 distinct chain · 44% helix, 21% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	D-ribulose-5-phosphate 3-epimerase, putative	protein	221	44% helix, 21% strand	Q8I5L3

Ligands and binding sites

ZN · Zinc ion · metal · 2 copies · chains A, B
SO4 · Sulfate ion · ion · 2 copies · chains A, B

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

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	87	0.62	0.89	25	SO4
2	87	0.62	0.90	25	SO4

Compared structures

1TQX · Crystal Structure of Pfal009167 A Putative D-Ribulose 5-Phosphate 3-Epimerase from… · 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 Q8I5L3
Elsewhere: RCSB PDB 1TQX · PDBe 1TQX · UniProt Q8I5L3

GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.