MolNFT v1 · #104826 · protein
Structure of the KRR1 and FAF1 complex from saccharomyces cerevisiae
4QMF · KRR1 small subunit processome component: “Structure of the KRR1 and FAF1 complex from saccharomyces cerevisiae”. X-ray diffraction, 2 pockets (best druggability 0.53). MolNFT v1 #104826 on GenesisL1: 3D structure, binding sites and…
- PDB
- 4QMF
- Type
- protein
- Length
- 389 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- KRR1 small subunit processome component; Protein FAF1
- UniProt
- P25586, P40546
- Pockets
- 2 · best druggability 0.53
Structure
x-ray diffraction · 3 distinct chains · 55% helix, 18% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| D | KRR1 small subunit processome component | protein | 174 | 53% helix, 18% strand | P25586 |
| B | KRR1 small subunit processome component | protein | 175 | 54% helix, 19% strand | P25586 |
| A, C | Protein FAF1 | protein | 20 | 85% helix, 0% strand | P40546 |
Pockets
2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 282 | 0.53 | 0.75 | 29 | empty |
| 2 | 137 | 0.46 | 0.77 | 22 | empty |
Interfaces
3 interfaces between chains.
- D–C · 545 Ų buried · 3 hydrogen bonds · protein-protein
- B–A · 542 Ų buried · 4 hydrogen bonds · protein-protein
- D–B · 346 Ų buried · 3 hydrogen bonds · protein-protein
Compared structures
- 4QMF · Structure of the Krr1 and Faf1 complex from Saccharomyces cerevisiae · the same entry in another collection · chain C against C, TM-score 1.00
- P25586 · AlphaFold monomer V2.0 prediction for KRR1 small subunit processome component (P25586) · a predicted model of the same protein · chain D against A, TM-score 0.99
- P40546 · AlphaFold monomer V2.0 prediction for protein FAF1 (P40546) · a predicted model of the same protein · chain C against A, TM-score 0.70
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 P25586
- Every structure of UniProt P40546
- Elsewhere: RCSB PDB 4QMF · PDBe 4QMF · UniProt P25586 · UniProt P40546
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