MolNFT v1 · #162314 · protein
Crystal structure of ppep-1(K101E/E184K)
6R56 · Pro-pro endopeptidase: “Crystal structure of ppep-1(K101E/E184K)”. X-ray diffraction, 1 ligand (ZN), 2 pockets (best druggability 0.74). MolNFT v1 #162314 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 6R56
- Type
- protein
- Length
- 388 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Pro-pro endopeptidase
- EC
- 3.4.24.89
- UniProt
- Q183R7
- Ligands
- ZN
- Pockets
- 2 · best druggability 0.74
Structure
x-ray diffraction · 2 distinct chains · 54% helix, 8% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Pro-pro endopeptidase (EC 3.4.24.89) | protein | 196 | 54% helix, 8% strand | Q183R7 |
| B | Pro-pro endopeptidase (EC 3.4.24.89) | protein | 192 | 55% helix, 8% strand | Q183R7 |
Ligands and binding sites
- ZN · Zinc ion · metal · 2 copies · chains A, B
- TRS · 2-amino-2-hydroxymethyl-propane-1,3-diol · additive · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 634 | 0.74 | 0.81 | 76 | TRS |
| 2 | 176 | 0.62 | 0.83 | 33 | TRS |
Interfaces
1 interface between chains.
- A–B · 538 Ų buried · 7 hydrogen bonds · protein-protein
Compared structures
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 Q183R7
- Elsewhere: RCSB PDB 6R56 · PDBe 6R56 · UniProt Q183R7
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