Research workbench
Crystal structure of human PCNA in complex with a traip peptide
Analyse Crystal structure of human PCNA in complex with a traip peptide in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4ZTD
- Type
- protein
- Length
- 787 residues
- Chains
- 6
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Proliferating cell nuclear antigen; Ala-phe-gln-ala-lys-leu-asp-thr-phe-leu-TRP-ser…
- UniProt
- P12004
- Pockets
- 5 · best druggability 0.47
Structure
x-ray diffraction · 4 distinct chains · 19% helix, 43% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Proliferating cell nuclear antigen | protein | 253 | 18% helix, 44% strand | P12004 |
| C | Proliferating cell nuclear antigen | protein | 252 | 20% helix, 45% strand | P12004 |
| D, E | Ala-phe-gln-ala-lys-leu-asp-thr-phe-leu-TRP-ser | protein | 12 | 25% helix, 0% strand | — |
| F | Ala-gly-ala-gly-ala | protein | 5 | 0% helix, 0% strand | — |
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 | 169 | 0.47 | 0.76 | 28 | empty |
| 2 | 157 | 0.43 | 0.75 | 21 | empty |
| 3 | 94 | 0.41 | 0.77 | 22 | empty |
| 4 | 107 | 0.40 | 0.76 | 24 | empty |
| 5 | 89 | 0.37 | 0.76 | 13 | empty |
Interfaces
6 interfaces between chains.
- A–B · 845 Ų buried · 17 hydrogen bonds · protein-protein
- A–C · 807 Ų buried · 17 hydrogen bonds · protein-protein
- B–C · 753 Ų buried · 16 hydrogen bonds · protein-protein
- A–E · 655 Ų buried · 10 hydrogen bonds · protein-protein
- B–D · 654 Ų buried · 7 hydrogen bonds · protein-protein
Compared structures
- 4ZTD · Crystal Structure of Human PCNA in complex with a TRAIP peptide · 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
- Elsewhere: RCSB PDB 4ZTD · PDBe 4ZTD · UniProt P12004
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