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Mouse RNF213 mutant R4753K modeling the moyamoya-disease-related human variant R4810K

Analyse Mouse RNF213 mutant R4753K modeling the moyamoya-disease-related human variant… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6TAY
Type: protein
Length: 4,417 residues
Chains: 1
Method: electron microscopy
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: RNF213,E3 ubiquitin-protein ligase RNF213,E3 ubiquitin- protein ligase RNF213
EC: 2.3.2.27, 3.6.4.-
UniProt: E9Q555
Ligands: ATP, ZN, MG
Pockets: 20 · best druggability 0.86

Structure

electron microscopy · 1 distinct chain · 53% helix, 6% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	RNF213,E3 ubiquitin-protein ligase RNF213,E3 ubiquitin- protein ligase RNF213 (EC 2.3.2.27, 3.6.4.-)	protein	4417	53% helix, 6% strand	E9Q555

Ligands and binding sites

ATP · Adenosine-5'-triphosphate · ligand · chains A
ZN · Zinc ion · metal · 2 copies · chains A
MG · Magnesium ion · metal · chains A

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

Pockets

20 pockets found on a 1 Å grid, 20 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	997	0.86	0.87	133	empty
2	1198	0.83	0.84	105	empty
3	1056	0.82	0.83	95	empty
4	910	0.79	0.81	93	empty
5	1019	0.77	0.79	85	empty

Modifications

Observed in the structure: 2 disulfide (disulfide).

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 E9Q555
Elsewhere: RCSB PDB 6TAY · PDBe 6TAY · UniProt E9Q555

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