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Co-crystal structure of carboxy cgmp binding domain of plasmodium falciparum pkg with cgmp

Analyse Co-crystal structure of carboxy cgmp binding domain of plasmodium falciparum… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4OFG
Type: protein
Length: 142 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Cgmp-dependent protein kinase
EC: 2.7.11.12
UniProt: Q8MMZ4
Ligands: N2P, PCG, SO4
Pockets: 1 · best druggability 0.71

Structure

x-ray diffraction · 1 distinct chain · 42% helix, 27% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Cgmp-dependent protein kinase (EC 2.7.11.12)	protein	142	42% helix, 27% strand	Q8MMZ4

Ligands and binding sites

N2P · Pentane-1,5-diamine · ligand · 6 copies · chains A
PCG · Cyclic guanosine monophosphate · ligand · chains A
SO4 · Sulfate ion · ion · 3 copies · chains A
EOH · Ethanol · additive · 13 copies · chains A

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

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	211	0.71	0.87	32	PCG, N2P, SO4, EOH

Compared structures

4OFG · Co-crystal structure of carboxy cGMP binding domain of Plasmodium falciparum PKG with cGMP · 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 Q8MMZ4
Elsewhere: RCSB PDB 4OFG · PDBe 4OFG · UniProt Q8MMZ4

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