MolNFT v1 · #29722 · protein
Complex of the S. cerevisiae ORC1 and SIR1 interacting domains
1ZHI · Origin recognition complex subunit 1: “Complex of the S. cerevisiae ORC1 and SIR1 interacting domains”. X-ray diffraction, 4 pockets (best druggability 0.57). MolNFT v1 #29722 on GenesisL1: 3D structure, binding sites and pockets in…
- PDB
- 1ZHI
- Type
- protein
- Length
- 320 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Origin recognition complex subunit 1; Regulatory protein SIR1
- UniProt
- P54784, P21691
- Pockets
- 4 · best druggability 0.57
Structure
x-ray diffraction · 2 distinct chains · 24% helix, 35% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Origin recognition complex subunit 1 | protein | 195 | 29% helix, 37% strand | P54784 |
| B | Regulatory protein SIR1 | protein | 125 | 18% helix, 32% strand | P21691 |
Pockets
4 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 265 | 0.57 | 0.78 | 38 | empty |
| 2 | 93 | 0.38 | 0.76 | 27 | empty |
| 3 | 71 | 0.35 | 0.76 | 19 | empty |
| 4 | 50 | 0.30 | 0.76 | 14 | empty |
Interfaces
1 interface between chains.
- A–B · 707 Ų buried · 10 hydrogen bonds · protein-protein
Compared structures
- 1ZHI · Complex of the S. cerevisiae Orc1 and Sir1 interacting domains · the same entry in another collection · chain A against A, TM-score 1.00
- 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 0.96
- P21691 · AlphaFold monomer V2.0 prediction for regulatory protein SIR1 (P21691) · a predicted model of the same protein · chain B against A, TM-score 0.96
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 1ZHI · PDBe 1ZHI · UniProt P54784 · UniProt P21691
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