Research workbench

AKAP18:PKA-riialpha structure reveals crucial anchor points for recognition of regulatory subunits of PKA

Analyse AKAP18:PKA-riialpha structure reveals crucial anchor points for recognition of… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4ZP3
Type: protein
Length: 652 residues
Chains: 18
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Camp-dependent protein kinase type II-alpha regulatory subunit; A-kinase anchor protein 7…
UniProt: P13861, O43687
Ligands: CD
Pockets: 6 · best druggability 0.85

Structure

x-ray diffraction · 9 distinct chains · 79% helix, 0% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, L	Camp-dependent protein kinase type II-alpha regulatory subunit	protein	43	67% helix, 0% strand	P13861
B, C, E	Camp-dependent protein kinase type II-alpha regulatory subunit	protein	39	74% helix, 0% strand	P13861
D, F, H, J	Camp-dependent protein kinase type II-alpha regulatory subunit	protein	41	71% helix, 0% strand	P13861
G	Camp-dependent protein kinase type II-alpha regulatory subunit	protein	42	71% helix, 0% strand	P13861
I, K	Camp-dependent protein kinase type II-alpha regulatory subunit	protein	38	79% helix, 0% strand	P13861
M	A-kinase anchor protein 7 isoforms alpha and beta	protein	28	93% helix, 0% strand	O43687
N	A-kinase anchor protein 7 isoforms alpha and beta	protein	28	89% helix, 0% strand	O43687
O, Q, R	A-kinase anchor protein 7 isoforms alpha and beta	protein	27	89% helix, 0% strand	O43687
P	A-kinase anchor protein 7 isoforms alpha and beta	protein	30	90% helix, 0% strand	O43687

Ligands and binding sites

CD · Cadmium ion · metal · 4 copies · chains A, D, I, B, C, J, F, G, E, H

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

Pockets

6 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	881	0.85	0.87	90	empty
2	298	0.75	0.87	44	empty
3	90	0.42	0.79	16	empty
4	72	0.37	0.77	19	empty
5	100	0.35	0.74	23	empty

Interfaces

43 interfaces between chains.

G–H · 1042 Å² buried · 7 hydrogen bonds · protein-protein
E–F · 965 Å² buried · 4 hydrogen bonds · protein-protein
A–B · 946 Å² buried · 2 hydrogen bonds · protein-protein
C–D · 942 Å² buried · 4 hydrogen bonds · protein-protein
K–L · 902 Å² buried · 2 hydrogen bonds · protein-protein

Compared structures

4ZP3 · AKAP18:PKA-RIIalpha structure reveals crucial anchor points for recognition of regulatory… · the same entry in another collection · chain J against J, TM-score 1.00

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 P13861
Every structure of UniProt O43687
Elsewhere: RCSB PDB 4ZP3 · PDBe 4ZP3 · UniProt P13861 · UniProt O43687

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