MolNFT v1 · #10479 · protein
Pyrococcus furiosus PCNA complexed with rfcl pip-box peptide
1ISQ · Proliferating cell nuclear antigen: “Pyrococcus furiosus PCNA complexed with rfcl pip-box peptide”. X-ray diffraction, 1 ligand (ACE), 2 pockets (best druggability 0.75). MolNFT v1 #10479 on GenesisL1: 3D structure, binding sites…
- PDB
- 1ISQ
- Type
- protein
- Length
- 248 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Proliferating cell nuclear antigen; Replication factor C large subunit
- UniProt
- O73947
- Ligands
- ACE
- Pockets
- 2 · best druggability 0.75
Structure
x-ray diffraction · 2 distinct chains · 20% helix, 46% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Proliferating cell nuclear antigen | protein | 240 | 19% helix, 48% strand | O73947 |
| B | Replication factor C large subunit | protein | 8 | 38% helix, 0% strand | — |
Ligands and binding sites
- ACE · Acetyl group · ligand · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
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 | 60 | 0.75 | 0.98 | 16 | empty |
| 2 | 109 | 0.38 | 0.75 | 19 | empty |
Interfaces
1 interface between chains.
- A–B · 488 Ų buried · 6 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 1 covalent (covalent ligand).
Compared structures
- 1ISQ · Pyrococcus furiosus PCNA complexed with RFCL PIP-box peptide · the same entry in another collection · chain A against A, TM-score 1.00
- O73947 · AlphaFold monomer V2.0 prediction for DNA polymerase sliding clamp (O73947) · a predicted model of the same protein · chain A against A, TM-score 0.97
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 O73947
- Elsewhere: RCSB PDB 1ISQ · PDBe 1ISQ · UniProt O73947
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