Research workbench
Structure of the chip-tpr domain in complex with the HSC70 lid-tail domains
Analyse Structure of the chip-tpr domain in complex with the HSC70 lid-tail domains in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4KBQ
- Type
- protein
- Length
- 434 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- E3 ubiquitin-protein ligase chip; Heat shock cognate 71 kda protein
- EC
- 6.3.2.-
- UniProt
- Q9UNE7, P11142
- Pockets
- 7 · best druggability 0.71
Structure
x-ray diffraction · 4 distinct chains · 74% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | E3 ubiquitin-protein ligase chip (EC 6.3.2.-) | protein | 130 | 75% helix, 0% strand | Q9UNE7 |
| B | E3 ubiquitin-protein ligase chip (EC 6.3.2.-) | protein | 126 | 78% helix, 0% strand | Q9UNE7 |
| D | Heat shock cognate 71 kda protein | protein | 87 | 72% helix, 0% strand | P11142 |
| C | Heat shock cognate 71 kda protein | protein | 91 | 70% helix, 0% strand | P11142 |
Pockets
7 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 523 | 0.71 | 0.80 | 53 | empty |
| 2 | 98 | 0.44 | 0.79 | 16 | empty |
| 3 | 77 | 0.35 | 0.77 | 18 | empty |
| 4 | 75 | 0.35 | 0.75 | 17 | empty |
| 5 | 111 | 0.34 | 0.72 | 10 | empty |
Interfaces
4 interfaces between chains.
- A–C · 1016 Ų buried · 17 hydrogen bonds · protein-protein
- B–D · 554 Ų buried · 13 hydrogen bonds · protein-protein
- A–D · 479 Ų buried · 2 hydrogen bonds · protein-protein
- A–B · 311 Ų buried · 1 hydrogen bond · protein-protein
Compared structures
- 4KBQ · Structure of the CHIP-TPR domain in complex with the Hsc70 Lid-Tail domains · the same entry in another collection · chain C against C, 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 A against A, TM-score 0.98
- P11142 · AlphaFold monomer V2.0 prediction for heat shock cognate 71 kda protein (P11142) · a predicted model of the same protein · chain C 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 Q9UNE7
- Every structure of UniProt P11142
- Elsewhere: RCSB PDB 4KBQ · PDBe 4KBQ · UniProt Q9UNE7 · UniProt P11142
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