Research workbench
P34-P44 complex
Analyse P34-P44 complex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5O85
- Type
- protein
- Length
- 490 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- Q13889, Q13888
- Ligands
- ZN
Structure
x-ray diffraction · 4 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 190 | — | Q13889 |
| B | — | protein | 49 | — | Q13888 |
| C | — | protein | 198 | — | Q13889 |
| D | — | protein | 53 | — | Q13888 |
Ligands and binding sites
- ZN · Zinc ion · metal · 4 copies · chains B, D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 5O85 · p34-p44 complex · the same entry in another collection · chain D against D, TM-score 1.00
- Q13889 · AlphaFold monomer V2.0 prediction for general transcription factor iih subunit 3 (Q13889) · a predicted model of the same protein · chain A against A, TM-score 0.98
- Q13888 · AlphaFold monomer V2.0 prediction for general transcription factor iih subunit 2 (Q13888) · a predicted model of the same protein · chain D against A, TM-score 0.93
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 Q13889
- Every structure of UniProt Q13888
- Elsewhere: RCSB PDB 5O85 · PDBe 5O85 · UniProt Q13889 · UniProt Q13888
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