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The closed state of RGLG1 vwa domain

Analyse The closed state of RGLG1 vwa domain in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6K89
Type: protein
Length: 282 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: E3 ubiquitin-protein ligase RGLG1
EC: 2.3.2.27
UniProt: Q9SS90
Ligands: MG, NA
Pockets: 1 · best druggability 0.44

Structure

x-ray diffraction · 1 distinct chain · 41% helix, 15% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
B	E3 ubiquitin-protein ligase RGLG1 (EC 2.3.2.27)	protein	282	41% helix, 15% strand	Q9SS90

Ligands and binding sites

MG · Magnesium ion · metal · chains B
NA · Sodium ion · metal · chains B

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

Pockets

1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	162	0.44	0.75	30	empty

Compared structures

6K89 · The closed state of RGLG1 VWA domain · the same entry in another collection · chain B against B, TM-score 1.00
Q9SS90 · AlphaFold monomer V2.0 prediction for E3 ubiquitin-protein ligase RGLG1 (Q9SS90) · a predicted model of the same protein · chain B against A, TM-score 0.92

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 Q9SS90
Elsewhere: RCSB PDB 6K89 · PDBe 6K89 · UniProt Q9SS90

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