Research workbench

Crystal structure of pelota C terminal domain from human

Analyse Crystal structure of pelota C terminal domain from human in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5EO3
Type: protein
Length: 201 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Protein pelota homolog
EC: 3.1.-.-
UniProt: Q9BRX2

Structure

x-ray diffraction · 2 distinct chains · 56% helix, 20% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Protein pelota homolog (EC 3.1.-.-)	protein	101	54% helix, 20% strand	Q9BRX2
B	Protein pelota homolog (EC 3.1.-.-)	protein	100	57% helix, 20% strand	Q9BRX2

Interfaces

1 interface between chains.

A–B · 496 Å² buried · 5 hydrogen bonds · protein-protein

Compared structures

5EO3 · Crystal Structure of Pelota C terminal domain from human · the same entry in another collection · chain A against A, TM-score 1.00
Q9BRX2 · AlphaFold monomer V2.0 prediction for protein pelota homolog (Q9BRX2) · a predicted model of the same protein · chain A against A, TM-score 0.96

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 Q9BRX2
Elsewhere: RCSB PDB 5EO3 · PDBe 5EO3 · UniProt Q9BRX2

GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.