Research workbench

Crystal structure of K39-acetylated SUMO1 in complex with pml-sim

Analyse Crystal structure of K39-acetylated SUMO1 in complex with pml-sim in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6UYP
Type: protein
Length: 90 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Small ubiquitin-related modifier 1; Protein pml
UniProt: P63165, P29590

Structure

x-ray diffraction · 2 distinct chains · 20% helix, 31% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Small ubiquitin-related modifier 1	protein	75	24% helix, 33% strand	P63165
B	Protein pml	protein	15	0% helix, 20% strand	P29590

Interfaces

1 interface between chains.

A–B · 474 Å² buried · 7 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 1 modified (acetylation).

Compared structures

6UYP · Crystal structure of K39-acetylated SUMO1 in complex with PML-SIM · the same entry in another collection · chain A against A, TM-score 1.00
P63165 · AlphaFold monomer V2.0 prediction for small ubiquitin-related modifier 1 (P63165) · a predicted model of the same protein · chain A against A, TM-score 0.97
P29590 · AlphaFold monomer V2.0 prediction for protein pml (P29590) · a predicted model of the same protein · chain B against A, TM-score 0.23

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 P63165
Every structure of UniProt P29590
Elsewhere: RCSB PDB 6UYP · PDBe 6UYP · UniProt P63165 · UniProt P29590

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