Research workbench

Crystal structure analysis of pyruvate kinase from bacillus stearothermophilus

Analyse Crystal structure analysis of pyruvate kinase from bacillus stearothermophilus in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2E28
Type: protein
Length: 587 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Pyruvate kinase
EC: 2.7.1.40
UniProt: Q02499
Ligands: SO4
Pockets: 7 · best druggability 0.67

Structure

x-ray diffraction · 1 distinct chain · 36% helix, 23% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Pyruvate kinase (EC 2.7.1.40)	protein	587	36% helix, 23% strand	Q02499

Ligands and binding sites

SO4 · Sulfate ion · ion · chains A

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

7 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	390	0.67	0.80	50	empty
2	73	0.65	0.92	26	SO4
3	203	0.55	0.79	25	empty
4	164	0.42	0.74	27	empty
5	67	0.37	0.78	16	empty

Compared structures

2E28 · Crystal structure analysis of pyruvate kinase from Bacillus stearothermophilus · the same entry in another collection · chain A against A, TM-score 1.00
Q02499 · AlphaFold monomer V2.0 prediction for pyruvate kinase (Q02499) · 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 Q02499
Elsewhere: RCSB PDB 2E28 · PDBe 2E28 · UniProt Q02499

GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.