MolNFT v1 · #28859 · protein
Structural and mechanistic analysis of two prolyl endopeptidases: role of inter-domain dynamics in catalysis and specificity
1YR2: “Structural and mechanistic analysis of two prolyl endopeptidases: role of inter-domain dynamics in catalysis…”. X-ray diffraction. MolNFT v1 #28859 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 1YR2
- Type
- protein
- Length
- 680 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- Q9ZNM8
Structure
x-ray diffraction · 1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 680 | — | Q9ZNM8 |
Compared structures
- 1YR2 · Structural and Mechanistic Analysis of Two Prolyl Endopeptidases: Role of Inter-Domain… · 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 Q9ZNM8
- Elsewhere: RCSB PDB 1YR2 · PDBe 1YR2 · UniProt Q9ZNM8
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.