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Solution NMR structure of the parkin ubl domain in complex with the endophilin-A1 SH3 domain

Analyse Solution NMR structure of the parkin ubl domain in complex with the… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2KNB
Type: protein
Length: 138 residues
Chains: 2
Method: solution nmr
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: E3 ubiquitin-protein ligase parkin; Endophilin-A1
EC: 6.3.2.-
UniProt: Q9JK66, O35179

Structure

solution nmr · 2 distinct chains · 15% helix, 39% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	E3 ubiquitin-protein ligase parkin (EC 6.3.2.-)	protein	76	24% helix, 34% strand	Q9JK66
B	Endophilin-A1	protein	62	5% helix, 45% strand	O35179

Interfaces

1 interface between chains.

A–B · 689 Å² buried · 11 hydrogen bonds · protein-protein

Compared structures

2KNB · Solution NMR structure of the parkin Ubl domain in complex with the endophilin-A1 SH3… · the same entry in another collection · chain A against A, TM-score 1.00
O35179 · AlphaFold monomer V2.0 prediction for endophilin-A1 (O35179) · a predicted model of the same protein · chain B against A, TM-score 0.95
Q9JK66 · AlphaFold monomer V2.0 prediction for E3 ubiquitin-protein ligase parkin (Q9JK66) · a predicted model of the same protein · chain A against A, TM-score 0.93

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 Q9JK66
Every structure of UniProt O35179
Elsewhere: RCSB PDB 2KNB · PDBe 2KNB · UniProt Q9JK66 · UniProt O35179

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