MolNFT v1 · #90581 · protein

Crystal structure of holoenzyme refined at 1.9 ångströms resolution: trigonal-bipyramidal geometry of the cation binding site

4ENL · Enolase: “Crystal structure of holoenzyme refined at 1.9 ångströms resolution: trigonal-bipyramidal geometry of the…”. X-ray diffraction, 2 ligands (ZN, SO4), 2 pockets (best druggability 0.56). MolNFT v1 #90581 on GenesisL1: 3D…

PDB: 4ENL
Type: protein
Length: 436 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Enolase
EC: 4.2.1.11
UniProt: P00924
Ligands: ZN, SO4
Pockets: 2 · best druggability 0.56

Structure

x-ray diffraction · 1 distinct chain · 45% helix, 17% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Enolase (EC 4.2.1.11)	protein	436	45% helix, 17% strand	P00924

Ligands and binding sites

ZN · Zinc ion · metal · chains A
SO4 · Sulfate ion · ion · 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, 1 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	255	0.56	0.78	40	SO4
2	73	0.40	0.79	20	empty

Compared structures

4ENL · Crystal structure of holoenzyme refined at 1.9 ångströms resolution: trigonal-bipyramidal… · the same entry in another collection · chain A against A, TM-score 1.00
P00924 · AlphaFold monomer V2.0 prediction for enolase 1 (P00924) · a predicted model of the same protein · chain A against A, TM-score 0.99

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 P00924
Elsewhere: RCSB PDB 4ENL · PDBe 4ENL · UniProt P00924

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