Research workbench
Structure of human T-complex protein 1 subunit epsilon (CCT5) mutant HIS147ARG
Analyse Structure of human T-complex protein 1 subunit epsilon (CCT5) mutant HIS147ARG in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5UYZ
- Type
- protein
- Length
- 1,928 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- T-complex protein 1 subunit epsilon
- UniProt
- P48643
- Ligands
- ADP, MG
- Pockets
- 20 · best druggability 0.79
Structure
x-ray diffraction · 4 distinct chains · 45% helix, 7% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | T-complex protein 1 subunit epsilon | protein | 493 | 45% helix, 8% strand | P48643 |
| B | T-complex protein 1 subunit epsilon | protein | 488 | 47% helix, 6% strand | P48643 |
| C | T-complex protein 1 subunit epsilon | protein | 488 | 44% helix, 7% strand | P48643 |
| D | T-complex protein 1 subunit epsilon | protein | 459 | 45% helix, 6% strand | P48643 |
Ligands and binding sites
- ADP · Adenosine-5'-diphosphate · ligand · 4 copies · chains A, B, C, D
- MG · Magnesium ion · metal · 3 copies · chains A, B, C
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
20 pockets found on a 1 Å grid, 12 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 527 | 0.79 | 0.86 | 52 | ADP, MG |
| 2 | 959 | 0.79 | 0.81 | 76 | empty |
| 3 | 1048 | 0.78 | 0.80 | 91 | ADP, MG |
| 4 | 906 | 0.77 | 0.80 | 76 | empty |
| 5 | 710 | 0.76 | 0.81 | 72 | ADP, MG |
Interfaces
5 interfaces between chains.
- C–D · 2128 Ų buried · 16 hydrogen bonds · protein-protein
- A–B · 1955 Ų buried · 21 hydrogen bonds · protein-protein
- B–C · 748 Ų buried · 7 hydrogen bonds · protein-protein
- A–D · 742 Ų buried · 7 hydrogen bonds · protein-protein
- B–D · 39 Ų buried · 0 hydrogen bonds · protein-protein
Compared structures
- 5UYZ · Structure of Human T-complex protein 1 subunit epsilon (CCT5) mutant His147Arg · the same entry in another collection · chain D against D, TM-score 1.00
- P48643 · AlphaFold monomer V2.0 prediction for T-complex protein 1 subunit epsilon (P48643) · a predicted model of the same protein · chain A 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 P48643
- Elsewhere: RCSB PDB 5UYZ · PDBe 5UYZ · UniProt P48643
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