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Crystal structure of the RNF20 ring domain

Analyse Crystal structure of the RNF20 ring domain in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5TRB
Type: protein
Length: 69 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: E3 ubiquitin-protein ligase BRE1A
EC: 6.3.2.-
UniProt: Q5VTR2
Ligands: ZN

Structure

x-ray diffraction · 1 distinct chain · 32% helix, 17% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	E3 ubiquitin-protein ligase BRE1A (EC 6.3.2.-)	protein	69	32% helix, 17% strand	Q5VTR2

Ligands and binding sites

ZN · Zinc ion · metal · 2 copies · chains A

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

Compared structures

5TRB · Crystal structure of the RNF20 RING domain · the same entry in another collection · chain A against A, TM-score 1.00
Q5VTR2 · AlphaFold monomer V2.0 prediction for E3 ubiquitin-protein ligase BRE1A (Q5VTR2) · a predicted model of the same protein · chain A against A, TM-score 0.95

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 Q5VTR2
Elsewhere: RCSB PDB 5TRB · PDBe 5TRB · UniProt Q5VTR2

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