MolNFT v2 · #150001 · protein
Structure of the PRO-PRO endopeptidase (PPEP-2) from Paenibacillus alvei
6FPC: “Structure of the PRO-PRO endopeptidase (PPEP-2) from Paenibacillus alvei”. X-ray diffraction at 1.75, 3 ligands (CD, ZN, SO4). MolNFT v2 #150001 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 6FPC
- Type
- protein
- Length
- 728 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 1.75
- Source
- Paenibacillus alvei
- UniProt
- K4ZRC1
- Ligands
- CD, ZN, SO4
Structure
x-ray diffraction · resolution 1.75 · 4 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 185 | — | K4ZRC1 |
| B | — | protein | 186 | — | K4ZRC1 |
| C | — | protein | 188 | — | K4ZRC1 |
| D | — | protein | 169 | — | K4ZRC1 |
Ligands and binding sites
- CD · Cadmium ion · metal · 14 copies · chains A, B, C, D
- ZN · Zinc ion · metal · 4 copies · chains A, B, C, D
- SO4 · Sulfate ion · ion · 14 copies · chains B, C, D, A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 6FPC · Structure of the pro-pro endopeptidase (ppep-2) from paenibacillus alvei · the same entry in another collection · chain D against D, TM-score 1.00
- K4ZRC1 · AlphaFold monomer V2.0 prediction for pro-pro endopeptidase (K4ZRC1) · a predicted model of the same protein · chain B against A, TM-score 0.99
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 K4ZRC1
- Elsewhere: RCSB PDB 6FPC · PDBe 6FPC · UniProt K4ZRC1
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