MolNFT v1 · #168768 · protein

HNRNPA2 low complexity domain (lcd) determined by cryoem

6WQK · Mcherry fluorescent PROTEIN,HETEROGENEOUS nuclear…: “HNRNPA2 low complexity domain (lcd) determined by cryoem”. Electron microscopy. MolNFT v1 #168768 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 6WQK
Type: protein
Length: 285 residues
Chains: 5
Method: electron microscopy
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Mcherry fluorescent PROTEIN,HETEROGENEOUS nuclear ribonucleoproteins A2/B1 chimera
UniProt: X5DSL3, P22626

Structure

electron microscopy · 1 distinct chain · 0% helix, 33% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B, C, D, E	Mcherry fluorescent PROTEIN,HETEROGENEOUS nuclear ribonucleoproteins A2/B1 chimera	protein	57	0% helix, 33% strand	X5DSL3, P22626

Interfaces

9 interfaces between chains.

B–C · 2313 Å² buried · 63 hydrogen bonds · protein-protein
A–B · 2304 Å² buried · 65 hydrogen bonds · protein-protein
A–E · 2301 Å² buried · 65 hydrogen bonds · protein-protein
D–E · 2296 Å² buried · 65 hydrogen bonds · protein-protein
A–C · 242 Å² buried · 3 hydrogen bonds · protein-protein

Compared structures

6WQK · hnRNPA2 Low complexity domain (LCD) determined by cryoEM · the same entry in another collection · chain E against E, TM-score 1.00
P22626 · AlphaFold monomer V2.0 prediction for heterogeneous nuclear ribonucleoproteins A2/B1… · a predicted model of the same protein · chain A against A, TM-score 0.29

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 X5DSL3
Every structure of UniProt P22626
Elsewhere: RCSB PDB 6WQK · PDBe 6WQK · UniProt X5DSL3 · UniProt P22626

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