MolNFT v2 · #180836 · protein
PanDDA analysis group deposition -- Aar2/RNaseH in complex with fragment P04D05 from the F2X-Universal Library
7FKG: “PanDDA analysis group deposition -- Aar2/RNaseH in complex with fragment P04D05 from the F2X-Universal Library”. X-ray diffraction at 1.51, 1 ligand (WOR). MolNFT v2 #180836 on GenesisL1: 3D structure, binding sites and pockets in…
- PDB
- 7FKG
- Type
- protein
- Length
- 537 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 1.51
- Source
- Saccharomyces cerevisiae S288C
- UniProt
- P33334, P32357
- Ligands
- WOR
Structure
x-ray diffraction · resolution 1.51 · 2 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 237 | — | P33334 |
| B | — | protein | 300 | — | P32357 |
Ligands and binding sites
- WOR · N'-(2-hydroxy-5-methylphenyl)-N-methyl-N-(propan-2-yl)sulfuric diamide · ligand · chains B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- P32357 · AlphaFold monomer V2.0 prediction for A1 cistron-splicing factor AAR2 (P32357) · a predicted model of the same protein · chain B against A, TM-score 1.00
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 P33334
- Every structure of UniProt P32357
- Elsewhere: RCSB PDB 7FKG · PDBe 7FKG · UniProt P33334 · UniProt P32357
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