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Crystal structure of phosphorylated SNF1 kinase domain

Analyse Crystal structure of phosphorylated SNF1 kinase domain in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3DAE
Type: protein
Length: 494 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Carbon catabolite-derepressing protein kinase
EC: 2.7.11.1
UniProt: P06782
Pockets: 3 · best druggability 0.71

Structure

x-ray diffraction · 2 distinct chains · 38% helix, 17% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Carbon catabolite-derepressing protein kinase (EC 2.7.11.1)	protein	248	38% helix, 17% strand	P06782
B	Carbon catabolite-derepressing protein kinase (EC 2.7.11.1)	protein	246	38% helix, 17% strand	P06782

Pockets

3 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	733	0.71	0.77	72	empty
2	606	0.67	0.77	53	empty
3	110	0.39	0.75	25	empty

Interfaces

1 interface between chains.

A–B · 811 Å² buried · 7 hydrogen bonds · protein-protein

Compared structures

3DAE · Crystal structure of phosphorylated SNF1 kinase domain · the same entry in another collection · chain A against A, TM-score 1.00
P06782 · AlphaFold monomer V2.0 prediction for carbon catabolite-derepressing protein kinase… · a predicted model of the same protein · chain B against A, TM-score 0.92

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 P06782
Elsewhere: RCSB PDB 3DAE · PDBe 3DAE · UniProt P06782

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