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Camp bound pfpka-R (297-441)

Analyse Camp bound pfpka-R (297-441) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5K8S
Type: protein
Length: 294 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Camp-dependent protein kinase regulatory subunit
UniProt: Q7KQK0
Ligands: CMP
Pockets: 3 · best druggability 0.69

Structure

x-ray diffraction · 2 distinct chains · 36% helix, 27% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Camp-dependent protein kinase regulatory subunit	protein	146	36% helix, 27% strand	Q7KQK0
B	Camp-dependent protein kinase regulatory subunit	protein	148	36% helix, 26% strand	Q7KQK0

Ligands and binding sites

CMP · Adenosine-3',5'-cyclic-monophosphate · ligand · 2 copies · chains A, B

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

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	242	0.69	0.85	38	CMP
2	292	0.67	0.82	42	CMP
3	116	0.39	0.75	26	empty

Interfaces

1 interface between chains.

A–B · 531 Å² buried · 11 hydrogen bonds · protein-protein

Compared structures

5K8S · cAMP bound PfPKA-R (297-441) · the same entry in another collection · chain B against B, 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 Q7KQK0
Elsewhere: RCSB PDB 5K8S · PDBe 5K8S · UniProt Q7KQK0

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