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Crystal structure of the T. brucei enolase complexed with phosphonoacetohydroxamate (pah), HIS156-in conformation

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

PDB: 2PU0
Type: protein
Length: 431 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Enolase
EC: 4.2.1.11
UniProt: Q38BV6
Ligands: PAH, ZN
Pockets: 1 · best druggability 0.32

Structure

x-ray diffraction · 1 distinct chain · 42% helix, 18% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Enolase (EC 4.2.1.11)	protein	431	42% helix, 18% strand	Q38BV6

Ligands and binding sites

PAH · Phosphonoacetohydroxamic acid · ligand · chains A
ZN · Zinc ion · metal · 3 copies · 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

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	69	0.32	0.75	18	empty

Compared structures

2PU0 · Crystal Structure of the T. brucei enolase complexed with phosphonoacetohydroxamate… · 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 2PU0 · PDBe 2PU0 · UniProt Q38BV6

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