MolNFT v1 · #127701 · protein
Prolyl oligopeptidase B from galerina marginata bound to 35MER hydrolysis and macrocyclization substrate - H698A mutant
5N4E: “Prolyl oligopeptidase B from galerina marginata bound to 35MER hydrolysis and macrocyclization substrate…”. X-ray diffraction. MolNFT v1 #127701 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 5N4E
- Type
- protein
- Length
- 1,482 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- H2E7Q8, H2E7Q5
Structure
x-ray diffraction · 4 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 714 | — | H2E7Q8 |
| B | — | protein | 707 | — | H2E7Q8 |
| C | — | protein | 30 | — | H2E7Q5 |
| D | — | protein | 31 | — | H2E7Q5 |
Ligands and binding sites
- GOL · Glycerol · additive · chains B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 5N4E · Prolyl oligopeptidase B from Galerina marginata bound to 35mer hydrolysis and… · the same entry in another collection · chain A against A, TM-score 1.00
- H2E7Q8 · AlphaFold monomer V2.0 prediction for dual function macrocyclase- peptidase popb (H2E7Q8) · a predicted model of the same protein · 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 H2E7Q8
- Every structure of UniProt H2E7Q5
- Elsewhere: RCSB PDB 5N4E · PDBe 5N4E · UniProt H2E7Q8 · UniProt H2E7Q5
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