Research workbench
Crystal structure of a Orc1p-Sir1p complex
Analyse Crystal structure of a Orc1p-Sir1p complex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1ZBX
- Type
- protein
- Length
- 317 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 2.5
- Source
- Saccharomyces cerevisiae
- Molecule
- Origin recognition complex subunit 1; Regulatory protein SIR1
- UniProt
- P54784, P21691
- Pockets
- 5 · best druggability 0.48
Structure
x-ray diffraction · resolution 2.5 · 2 distinct chains · 24% helix, 35% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Origin recognition complex subunit 1 | protein | 197 | 26% helix, 36% strand | P54784 |
| B | Regulatory protein SIR1 | protein | 120 | 19% helix, 34% strand | P21691 |
Pockets
5 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 183 | 0.48 | 0.76 | 37 | empty |
| 2 | 191 | 0.48 | 0.75 | 20 | empty |
| 3 | 91 | 0.38 | 0.76 | 19 | empty |
| 4 | 77 | 0.35 | 0.76 | 14 | empty |
| 5 | 55 | 0.30 | 0.75 | 18 | empty |
Interfaces
1 interface between chains.
- A–B · 676 Ų buried · 8 hydrogen bonds · protein-protein
Compared structures
- 1ZBX · Crystal structure of a ORC1P-SIR1P complex · the same entry in another collection · chain A against A, TM-score 1.00
- P21691 · AlphaFold monomer V2.0 prediction for regulatory protein SIR1 (P21691) · a predicted model of the same protein · chain B against A, TM-score 0.97
- P54784 · AlphaFold monomer V2.0 prediction for origin recognition complex subunit 1 (P54784) · a predicted model of the same protein · chain A against A, TM-score 0.94
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 P54784
- Every structure of UniProt P21691
- Elsewhere: RCSB PDB 1ZBX · PDBe 1ZBX · UniProt P54784 · UniProt P21691
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