Research workbench
Crystal structure of the nemo cozi in complex with hoip NZF1 domain
Analyse Crystal structure of the nemo cozi in complex with hoip NZF1 domain in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4OWF
- Type
- protein
- Length
- 198 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Nf-kappa-B essential modulator; E3 ubiquitin-protein ligase RNF31
- EC
- 6.3.2.-
- UniProt
- O88522, Q96EP0
- Ligands
- ZN
Structure
x-ray diffraction · 3 distinct chains · 82% helix, 3% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Nf-kappa-B essential modulator (EC 6.3.2.-) | protein | 83 | 96% helix, 0% strand | O88522 |
| B | Nf-kappa-B essential modulator (EC 6.3.2.-) | protein | 86 | 97% helix, 0% strand | O88522 |
| G | E3 ubiquitin-protein ligase RNF31 (EC 6.3.2.-) | protein | 29 | 0% helix, 21% strand | Q96EP0 |
Ligands and binding sites
- ZN · Zinc ion · metal · chains G
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Interfaces
3 interfaces between chains.
- A–B · 2421 Ų buried · 9 hydrogen bonds · protein-protein
- B–G · 359 Ų buried · 5 hydrogen bonds · protein-protein
- A–G · 231 Ų buried · 3 hydrogen bonds · protein-protein
Compared structures
- 4OWF · Crystal structure of the NEMO CoZi in complex with HOIP NZF1 domain · the same entry in another collection · chain A against A, TM-score 1.00
- Q96EP0 · AlphaFold monomer V2.0 prediction for E3 ubiquitin-protein ligase RNF31 (Q96EP0) · a predicted model of the same protein · chain G against A, TM-score 0.91
- O88522 · AlphaFold monomer V2.0 prediction for nf-kappa-B essential modulator (O88522) · a predicted model of the same protein · chain A against A, TM-score 0.81
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 O88522
- Every structure of UniProt Q96EP0
- Elsewhere: RCSB PDB 4OWF · PDBe 4OWF · UniProt O88522 · UniProt Q96EP0
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