MolNFT v1 · #24118 · protein
Crystal structure of the human FEN1-PCNA complex
1UL1 · Flap endonuclease-1: “Crystal structure of the human FEN1-PCNA complex”. X-ray diffraction, 1 ligand (MG), 20 pockets (best druggability 0.69). MolNFT v1 #24118 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 1UL1
- Type
- protein
- Length
- 1,743 residues
- Chains
- 6
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Flap endonuclease-1; Proliferating cell nuclear antigen
- UniProt
- P39748, P12004
- Ligands
- MG
- Pockets
- 20 · best druggability 0.69
Structure
x-ray diffraction · 6 distinct chains · 30% helix, 25% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| X | Flap endonuclease-1 | protein | 313 | 44% helix, 11% strand | P39748 |
| Y | Flap endonuclease-1 | protein | 312 | 40% helix, 11% strand | P39748 |
| Z | Flap endonuclease-1 | protein | 349 | 34% helix, 9% strand | P39748 |
| A | Proliferating cell nuclear antigen | protein | 256 | 18% helix, 46% strand | P12004 |
| B | Proliferating cell nuclear antigen | protein | 258 | 17% helix, 43% strand | P12004 |
| C | Proliferating cell nuclear antigen | protein | 255 | 20% helix, 44% strand | P12004 |
Ligands and binding sites
- MG · Magnesium ion · metal · 4 copies · chains X, Y
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
20 pockets found on a 1 Å grid, 9 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 420 | 0.69 | 0.81 | 54 | empty |
| 2 | 197 | 0.66 | 0.85 | 31 | empty |
| 3 | 413 | 0.59 | 0.75 | 52 | empty |
| 4 | 109 | 0.58 | 0.85 | 23 | empty |
| 5 | 203 | 0.58 | 0.80 | 30 | empty |
Interfaces
6 interfaces between chains.
- X–A · 1824 Ų buried · 35 hydrogen bonds · protein-protein
- Y–B · 1495 Ų buried · 21 hydrogen bonds · protein-protein
- Z–C · 1307 Ų buried · 20 hydrogen bonds · protein-protein
- A–B · 758 Ų buried · 12 hydrogen bonds · protein-protein
- B–C · 747 Ų buried · 16 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 1 disulfide (disulfide).
Compared structures
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 P39748
- Every structure of UniProt P12004
- Elsewhere: RCSB PDB 1UL1 · PDBe 1UL1 · UniProt P39748 · UniProt P12004
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