Research workbench
Origin Recognition Complex Associated (ORCA) protein bound to Orc2
Analyse Origin Recognition Complex Associated (ORCA) protein bound to Orc2 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 8SIU
- Type
- protein
- Length
- 386 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 1.8
- Source
- Rattus norvegicus
- Molecule
- Leucine-rich repeat and WD repeat-containing protein 1; Origin recognition complex…
- UniProt
- A0A140UHX1, Q75PQ8
- Ligands
- SO4
- Pockets
- 3 · best druggability 0.76
Structure
x-ray diffraction · resolution 1.8 · 2 distinct chains · 4% helix, 47% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Leucine-rich repeat and WD repeat-containing protein 1 | protein | 368 | 5% helix, 48% strand | A0A140UHX1 |
| B | Origin recognition complex subunit 2 | protein | 18 | 0% helix, 28% strand | Q75PQ8 |
Ligands and binding sites
- SO4 · Sulfate ion · ion · 2 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, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 848 | 0.76 | 0.80 | 52 | empty |
| 2 | 103 | 0.54 | 0.84 | 28 | empty |
| 3 | 99 | 0.53 | 0.83 | 19 | empty |
Interfaces
1 interface between chains.
- A–B · 1002 Ų buried · 15 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 3 modified (engineered).
Compared structures
- Q75PQ8 · AlphaFold monomer V2.0 prediction for origin recognition complex subunit 2 (Q75PQ8) · a predicted model of the same protein · chain B against A, TM-score 0.26
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 A0A140UHX1
- Every structure of UniProt Q75PQ8
- Elsewhere: RCSB PDB 8SIU · PDBe 8SIU · UniProt A0A140UHX1 · UniProt Q75PQ8
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