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Solution structure of the docking and dimerization domain of the type I alpha regulatory subunit of protein kinase a (rialpha D/D)

Analyse Solution structure of the docking and dimerization domain of the type I alpha… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2EZW
Type: protein
Length: 100 residues
Chains: 2
Method: solution nmr
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Camp-dependent protein kinase type I-alpha regulatory subunit
EC: 2.7.1.37
UniProt: P00514
Pockets: 1 · best druggability 0.39

Structure

solution nmr · 1 distinct chain · 56% helix, 0% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Camp-dependent protein kinase type I-alpha regulatory subunit (EC 2.7.1.37)	protein	50	56% helix, 0% strand	P00514

Pockets

1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	137	0.39	0.73	18	empty

Interfaces

1 interface between chains.

A–B · 1131 Å² buried · 0 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 2 disulfide (disulfide).

Compared structures

2EZW · Solution structure of the docking and dimerization domain of the type I alpha regulatory… · the same entry in another collection · chain A against A, TM-score 1.00
P00514 · AlphaFold monomer V2.0 prediction for camp-dependent protein kinase type I-alpha… · a predicted model of the same protein · chain A against A, TM-score 0.51

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 P00514
Elsewhere: RCSB PDB 2EZW · PDBe 2EZW · UniProt P00514

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