Research workbench

Inhibiting parasite proliferation using a rationally designed anti- tubulin agent

Analyse Inhibiting parasite proliferation using a rationally designed anti- tubulin… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 7PJE
Type: protein
Length: 1,946 residues
Chains: 6
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
UniProt: P41351, P41352
Ligands: GTP, MG

Structure

x-ray diffraction · 6 distinct chains.

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	—	protein	422	—	P41351
B	—	protein	425	—	P41352
F	—	protein	126	—	—
C	—	protein	424	—	P41351
D	—	protein	424	—	P41352
E	—	protein	125	—	—

Ligands and binding sites

GTP · Guanosine-5'-triphosphate · ligand · 4 copies · chains A, B, C, D
MG · Magnesium ion · metal · 3 copies · chains B

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

Compared structures

7PJE · Inhibiting parasite proliferation using a rationally designed anti-tubulin agent · the same entry in another collection · chain E against E, TM-score 1.00
P41351 · AlphaFold monomer V2.0 prediction for tubulin alpha chain (P41351) · a predicted model of the same protein · chain A against A, TM-score 0.99
P41352 · AlphaFold monomer V2.0 prediction for tubulin beta chain (P41352) · a predicted model of the same protein · chain D against A, TM-score 0.97

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 P41351
Every structure of UniProt P41352
Elsewhere: RCSB PDB 7PJE · PDBe 7PJE · UniProt P41351 · UniProt P41352

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