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Crystal structure of the rgs domain of CG5036

Analyse Crystal structure of the rgs domain of CG5036 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4IGU
Type: protein
Length: 274 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: CG5036
UniProt: Q8T017
Ligands: NA, CL
Pockets: 5 · best druggability 0.61

Structure

x-ray diffraction · 1 distinct chain · 64% helix, 0% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	CG5036	protein	137	64% helix, 0% strand	Q8T017

Ligands and binding sites

NA · Sodium ion · metal · 2 copies · chains A, B
CL · Chloride ion · ion · 5 copies · chains A, B
EDO · 1,2-ethanediol · additive · chains A, B

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

Pockets

5 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	274	0.61	0.80	29	CL
2	91	0.45	0.80	22	empty
3	102	0.44	0.79	20	NA, EDO
4	108	0.43	0.78	20	CL
5	76	0.39	0.79	17	NA, CL

Interfaces

1 interface between chains.

A–B · 766 Å² buried · 12 hydrogen bonds · protein-protein

Compared structures

4IGU · Crystal structure of the RGS domain of CG5036 · 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 Q8T017
Elsewhere: RCSB PDB 4IGU · PDBe 4IGU · UniProt Q8T017

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