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Crystal structure of a cAMP sensor G-Flamp1.

Analyse Crystal structure of a cAMP sensor G-Flamp1. in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6M63
Type: protein
Length: 717 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v2 / PDB Bank
Contract: 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
Owner: 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
Resolution: 2.25
Source: Aequorea victoria; Mesorhizobium japonicum MAFF 303099
Molecule: Chimera of Cyclic nucleotide-gated potassium channel mll3241 and Yellow fluorescent…
UniProt: Q98GN8, A0A059PIR9
Ligands: CMP
Pockets: 7 · best druggability 0.77

Structure

x-ray diffraction · resolution 2.25 · 2 distinct chains · 23% helix, 43% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Chimera of Cyclic nucleotide-gated potassium channel mll3241 and Yellow fluorescent protein	protein	359	23% helix, 43% strand	Q98GN8, A0A059PIR9
B	Chimera of Cyclic nucleotide-gated potassium channel mll3241 and Yellow fluorescent protein	protein	358	22% helix, 43% strand	Q98GN8, A0A059PIR9

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

7 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	93	0.77	0.97	28	empty
2	87	0.76	0.98	24	empty
3	741	0.75	0.80	64	empty
4	406	0.70	0.81	49	CMP
5	263	0.70	0.85	38	CMP

Interfaces

1 interface between chains.

A–B · 512 Å² buried · 5 hydrogen bonds · protein-protein

Compared structures

6M63 · Crystal structure of a camp sensor G-FLAMP1. · the same entry in another collection · chain A against A, TM-score 1.00
Q98GN8 · AlphaFold monomer V2.0 prediction for cyclic nucleotide-gated potassium channel MLL3241… · a predicted model of the same protein · chain B against A, TM-score 0.36

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 Q98GN8
Every structure of UniProt A0A059PIR9
Elsewhere: RCSB PDB 6M63 · PDBe 6M63 · UniProt Q98GN8 · UniProt A0A059PIR9

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