Research workbench
Crystal structure of the human chip tpr domain in complex with a 5MER acetylated optimized peptide
Analyse Crystal structure of the human chip tpr domain in complex with a 5MER… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6NSV
- Type
- protein
- Length
- 268 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- Q9UNE7
- Ligands
- ACE, NA, CL
Structure
x-ray diffraction · 3 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 128 | — | Q9UNE7 |
| B | — | protein | 130 | — | Q9UNE7 |
| C, D | — | protein | 5 | — | — |
Ligands and binding sites
- ACE · Acetyl group · ligand · 2 copies · chains A, C, B, D
- NA · Sodium ion · metal · 2 copies · chains A, B
- CL · Chloride ion · ion · chains A
- 1PE · Pentaethylene glycol · additive · 2 copies · chains A, B, C, D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 6NSV · Crystal structure of the human CHIP TPR domain in complex with a 5mer acetylated… · the same entry in another collection · chain A against A, TM-score 1.00
- Q9UNE7 · AlphaFold monomer V2.0 prediction for E3 ubiquitin-protein ligase chip (Q9UNE7) · a predicted model of the same protein · chain B against A, TM-score 0.99
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 Q9UNE7
- Elsewhere: RCSB PDB 6NSV · PDBe 6NSV · UniProt Q9UNE7
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