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Crystal Structure of the T. brucei enolase complexed with PEP

Analyse Crystal Structure of the T. brucei enolase complexed with PEP in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2PTY
Type: protein
Length: 431 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v2 / PDB Bank
Contract: 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
Owner: 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
Resolution: 2
Source: Trypanosoma brucei
Molecule: Enolase
EC: 4.2.1.11
UniProt: Q38BV6
Ligands: PEP, ZN
Pockets: 2 · best druggability 0.31

Structure

x-ray diffraction · resolution 2 · 1 distinct chain · 42% helix, 17% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Enolase (EC 4.2.1.11)	protein	431	42% helix, 17% strand	Q38BV6

Ligands and binding sites

PEP · Phosphoenolpyruvate · ligand · chains A
ZN · Zinc ion · metal · 2 copies · chains A
EDO · 1,2-ethanediol · additive · 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, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	68	0.31	0.75	18	empty
2	60	0.29	0.74	18	empty

Compared structures

2PTY · Crystal structure of the T. brucei enolase complexed with pep · 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 Q38BV6
Elsewhere: RCSB PDB 2PTY · PDBe 2PTY · UniProt Q38BV6

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