MolNFT v1 · #25549 · protein
Structural and biochemical studies of human PCNA complexes provide the basis for association with CDK/CYCLIN and rationale for inhibitor design
1VYJ: “Structural and biochemical studies of human PCNA complexes provide the basis for association with CDK/CYCLIN…”. X-ray diffraction. MolNFT v1 #25549 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 1VYJ
- Type
- protein
- Length
- 1,641 residues
- Chains
- 12
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P12004
Structure
x-ray diffraction · 3 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, C, E, I, K | — | protein | 257 | — | P12004 |
| B, D, F, H, J, L | — | protein | 16 | — | — |
| G | — | protein | 260 | — | P12004 |
Compared structures
- 1VYJ · Structural and biochemical studies of human PCNA complexes provide the basis for… · 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 1VYJ · PDBe 1VYJ · UniProt P12004
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