MolNFT v1 · #19466 · protein

The catalytic mechanism of phosphorylase kinase probed by mutational studies

1QL6: “The catalytic mechanism of phosphorylase kinase probed by mutational studies”. X-ray diffraction, 3 ligands (ATP, MN, SO4), 1 pocket (best druggability 0.66). MolNFT v1 #19466 on GenesisL1: 3D structure, binding sites and pockets in…

PDB: 1QL6
Type: protein
Length: 281 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Phosphorylase kinase
EC: 2.7.1.38
UniProt: P00518
Ligands: ATP, MN, SO4
Pockets: 1 · best druggability 0.66

Structure

x-ray diffraction · 1 distinct chain · 41% helix, 19% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Phosphorylase kinase (EC 2.7.1.38)	protein	281	41% helix, 19% strand	P00518

Ligands and binding sites

ATP · Adenosine-5'-triphosphate · ligand · chains A
MN · Manganese (II) ion · metal · 2 copies · chains A
SO4 · Sulfate ion · ion · 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	373	0.66	0.80	40	ATP, MN

Compared structures

1QL6 · The catalytic mechanism of phosphorylase kinase probed by mutational studies · the same entry in another collection · chain A against A, TM-score 1.00
P00518 · AlphaFold monomer V2.0 prediction for phosphorylase B kinase gamma catalytic chain… · 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 P00518
Elsewhere: RCSB PDB 1QL6 · PDBe 1QL6 · UniProt P00518

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