Research workbench
Human PCNA variant (S228I) complexed with FEN1 at 2.1 ångströms
Analyse Human PCNA variant (S228I) complexed with FEN1 at 2.1 ångströms in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5E0V
- Type
- protein
- Length
- 523 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Proliferating cell nuclear antigen; Flap endonuclease 1
- EC
- 3.1.-.-
- UniProt
- P12004, B4DWZ4
- Pockets
- 3 · best druggability 0.57
Structure
x-ray diffraction · 4 distinct chains · 21% helix, 43% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Proliferating cell nuclear antigen | protein | 249 | 21% helix, 44% strand | P12004 |
| B | Proliferating cell nuclear antigen | protein | 247 | 21% helix, 45% strand | P12004 |
| C | Flap endonuclease 1 (EC 3.1.-.-) | protein | 14 | 21% helix, 14% strand | B4DWZ4 |
| D | Flap endonuclease 1 (EC 3.1.-.-) | protein | 13 | 23% helix, 15% strand | B4DWZ4 |
Pockets
3 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 198 | 0.57 | 0.80 | 26 | empty |
| 2 | 56 | 0.48 | 0.85 | 17 | empty |
| 3 | 70 | 0.39 | 0.79 | 23 | empty |
Interfaces
4 interfaces between chains.
- A–C · 779 Ų buried · 14 hydrogen bonds · protein-protein
- B–D · 741 Ų buried · 14 hydrogen bonds · protein-protein
- A–D · 450 Ų buried · 10 hydrogen bonds · protein-protein
- A–B · 380 Ų buried · 4 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 2 disulfide (disulfide).
Compared structures
- 5E0V · Human PCNA variant (S228I) complexed with FEN1 at 2.1 Angstroms · the same entry in another collection · chain A against A, TM-score 1.00
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 P12004
- Every structure of UniProt B4DWZ4
- Elsewhere: RCSB PDB 5E0V · PDBe 5E0V · UniProt P12004 · UniProt B4DWZ4
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