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Crystal structure of human enolase-phosphatase E1

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

PDB: 1ZS9
Type: protein
Length: 253 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: E-1 enzyme
UniProt: Q9UHY7
Ligands: MG
Pockets: 1 · best druggability 0.59

Structure

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

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	E-1 enzyme	protein	253	52% helix, 12% strand	Q9UHY7

Ligands and binding sites

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	165	0.59	0.82	29	MG

Modifications

Observed in the structure: 5 modified (engineered).

Compared structures

1ZS9 · Crystal structure of human enolase-phosphatase E1 · 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 1ZS9 · PDBe 1ZS9 · UniProt Q9UHY7

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