Research workbench
Crystal structure of TAX1BP1 skich region in complex with NAP1
Analyse Crystal structure of TAX1BP1 skich region in complex with NAP1 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5Z7G
- Type
- protein
- Length
- 305 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- TAX1-binding protein 1; 5-azacytidine-induced protein 2
- UniProt
- Q86VP1, Q9H6S1
Structure
x-ray diffraction · 3 distinct chains · 18% helix, 34% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | TAX1-binding protein 1 | protein | 110 | 5% helix, 42% strand | Q86VP1 |
| B | TAX1-binding protein 1 | protein | 109 | 3% helix, 40% strand | Q86VP1 |
| C, D | 5-azacytidine-induced protein 2 | protein | 43 | 88% helix, 0% strand | Q9H6S1 |
Ligands and binding sites
- GOL · Glycerol · additive · 3 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Interfaces
5 interfaces between chains.
- C–D · 1122 Ų buried · 15 hydrogen bonds · protein-protein
- A–D · 648 Ų buried · 4 hydrogen bonds · protein-protein
- B–C · 543 Ų buried · 1 hydrogen bond · protein-protein
- B–D · 316 Ų buried · 3 hydrogen bonds · protein-protein
- A–C · 306 Ų buried · 2 hydrogen bonds · protein-protein
Compared structures
- 5Z7G · Crystal structure of TAX1BP1 SKICH region in complex with NAP1 · the same entry in another collection · chain D against D, TM-score 1.00
- Q86VP1 · AlphaFold monomer V2.0 prediction for TAX1-binding protein 1 (Q86VP1) · a predicted model of the same protein · chain B against A, TM-score 0.97
- Q9H6S1 · AlphaFold monomer V2.0 prediction for 5-azacytidine-induced protein 2 (Q9H6S1) · a predicted model of the same protein · chain D against A, TM-score 0.91
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 Q86VP1
- Every structure of UniProt Q9H6S1
- Elsewhere: RCSB PDB 5Z7G · PDBe 5Z7G · UniProt Q86VP1 · UniProt Q9H6S1
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