MolNFT v1 · #16976 · protein

Structure of trypanosoma brucei enolase reveals the inhibitory divalent metal site

1OEP: “Structure of trypanosoma brucei enolase reveals the inhibitory divalent metal site”. X-ray diffraction, 2 ligands (ZN, SO4), 3 pockets (best druggability 0.57). MolNFT v1 #16976 on GenesisL1: 3D structure, binding sites and pockets…

PDB: 1OEP
Type: protein
Length: 422 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Enolase
EC: 4.2.1.11
UniProt: Q9NDH8
Ligands: ZN, SO4
Pockets: 3 · best druggability 0.57

Structure

x-ray diffraction · 1 distinct chain · 41% helix, 17% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Enolase (EC 4.2.1.11)	protein	422	41% helix, 17% strand	Q9NDH8

Ligands and binding sites

ZN · Zinc ion · metal · 2 copies · chains A
SO4 · Sulfate ion · ion · chains A
EDO · 1,2-ethanediol · additive · 3 copies · chains A

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

Pockets

3 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	180	0.57	0.81	30	SO4
2	71	0.33	0.75	21	empty
3	75	0.32	0.74	18	empty

Compared structures

1OEP · Structure of Trypanosoma brucei enolase reveals the inhibitory divalent metal site · 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 Q9NDH8
Elsewhere: RCSB PDB 1OEP · PDBe 1OEP · UniProt Q9NDH8

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