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Crystal structure of cgmp bound cgmp-dependent protein KINASE(92-227)

Analyse Crystal structure of cgmp bound cgmp-dependent protein KINASE(92-227) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3OD0
Type: protein
Length: 254 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: PRKG1 protein
EC: 2.7.11.12
UniProt: Q6P5T7
Ligands: PCG
Pockets: 4 · best druggability 0.72

Structure

x-ray diffraction · 1 distinct chain · 26% helix, 31% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	PRKG1 protein (EC 2.7.11.12)	protein	127	26% helix, 31% strand	Q6P5T7

Ligands and binding sites

PCG · Cyclic guanosine monophosphate · ligand · 2 copies · chains A, B

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

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	264	0.72	0.86	27	PCG
2	142	0.49	0.78	22	PCG
3	76	0.34	0.76	19	empty
4	50	0.25	0.73	15	empty

Interfaces

1 interface between chains.

A–B · 765 Å² buried · 3 hydrogen bonds · protein-protein

Compared structures

3OD0 · Crystal structure of cGMP bound cGMP-dependent protein kinase(92-227) · the same entry in another collection · chain A against A, 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 Q6P5T7
Elsewhere: RCSB PDB 3OD0 · PDBe 3OD0 · UniProt Q6P5T7

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