MolNFT v1 · #142254 · protein
Structure of the yeast CTR9/PAF1 complex
5ZYP · RNA polymerase-associated protein CTR9,RNA polymerase II…: “Structure of the yeast CTR9/PAF1 complex”. X-ray diffraction, 1 ligand (NI), 3 pockets (best druggability 0.67). MolNFT v1 #142254 on GenesisL1: 3D structure, binding sites…
- PDB
- 5ZYP
- Type
- protein
- Length
- 340 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- RNA polymerase-associated protein CTR9,RNA polymerase II- associated protein 1
- UniProt
- P89105, P38351
- Ligands
- NI
- Pockets
- 3 · best druggability 0.67
Structure
x-ray diffraction · 1 distinct chain · 64% helix, 3% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | RNA polymerase-associated protein CTR9,RNA polymerase II- associated protein 1 | protein | 340 | 64% helix, 3% strand | P89105, P38351 |
Ligands and binding sites
- NI · Nickel (II) ion · metal · 3 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 638 | 0.67 | 0.77 | 63 | empty |
| 2 | 72 | 0.42 | 0.80 | 15 | empty |
| 3 | 125 | 0.40 | 0.74 | 23 | empty |
Modifications
Observed in the structure: 7 modified (engineered).
Compared structures
- 5ZYP · Structure of the Yeast Ctr9/Paf1 complex · the same entry in another collection · chain A against A, TM-score 1.00
- P89105 · AlphaFold monomer V2.0 prediction for RNA polymerase-associated protein CTR9 (P89105) · a predicted model of the same protein · chain A against A, TM-score 0.79
- P38351 · AlphaFold monomer V2.0 prediction for RNA polymerase II-associated protein 1 (P38351) · a predicted model of the same protein · chain A against A, TM-score 0.20
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 P89105
- Every structure of UniProt P38351
- Elsewhere: RCSB PDB 5ZYP · PDBe 5ZYP · UniProt P89105 · UniProt P38351
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