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Crystal structure of enolase from synechococcus elongatus

Analyse Crystal structure of enolase from synechococcus elongatus in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4ROP
Type: protein
Length: 424 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Enolase
EC: 4.2.1.11
UniProt: Q5N3P4
Ligands: CA
Pockets: 2 · best druggability 0.46

Structure

x-ray diffraction · 1 distinct chain · 43% helix, 20% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Enolase (EC 4.2.1.11)	protein	424	43% helix, 20% strand	Q5N3P4

Ligands and binding sites

CA · Calcium ion · metal · 4 copies · 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, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	152	0.46	0.77	28	empty
2	50	0.23	0.72	15	empty

Compared structures

4ROP · Crystal structure of enolase from Synechococcus elongatus · the same entry in another collection · chain A against A, TM-score 1.00
Q5N3P4 · AlphaFold monomer V2.0 prediction for enolase (Q5N3P4) · a predicted model of the same protein · chain A against A, TM-score 0.98

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 Q5N3P4
Elsewhere: RCSB PDB 4ROP · PDBe 4ROP · UniProt Q5N3P4

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