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Crystal structure of human enolase-phosphatase E1 and its complex with a substrate analog

Analyse Crystal structure of human enolase-phosphatase E1 and its complex with a… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1YNS
Type: protein
Length: 254 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: E-1 enzyme
UniProt: Q9UHY7
Ligands: HPO, MG
Pockets: 1 · best druggability 0.62

Structure

x-ray diffraction · 1 distinct chain · 52% helix, 12% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	E-1 enzyme	protein	254	52% helix, 12% strand	Q9UHY7

Ligands and binding sites

HPO · 2-oxoheptylphosphonic acid · ligand · chains A
MG · Magnesium ion · metal · 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, 1 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	158	0.62	0.84	29	MG, HPO

Compared structures

1YNS · Crystal Structure Of Human Enolase-phosphatase E1 and its complex with a substrate analog · the same entry in another collection · chain A against A, TM-score 1.00
Q9UHY7 · AlphaFold monomer V2.0 prediction for enolase-phosphatase E1 (Q9UHY7) · 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 Q9UHY7
Elsewhere: RCSB PDB 1YNS · PDBe 1YNS · UniProt Q9UHY7

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