MolNFT v1 · #112946 · protein
Apo-structure of metalloprotease ZMP1 from clostridium difficile
5A0P · Zinc metalloprotease ZMP1: “Apo-structure of metalloprotease ZMP1 from clostridium difficile”. X-ray diffraction, 1 ligand (ZN), 3 pockets (best druggability 0.71). MolNFT v1 #112946 on GenesisL1: 3D structure, binding sites and…
- PDB
- 5A0P
- Type
- protein
- Length
- 390 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Zinc metalloprotease ZMP1
- EC
- 3.4.24.-
- UniProt
- Q183R7
- Ligands
- ZN
- Pockets
- 3 · best druggability 0.71
Structure
x-ray diffraction · 1 distinct chain · 53% helix, 8% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Zinc metalloprotease ZMP1 (EC 3.4.24.-) | protein | 195 | 53% helix, 8% strand | Q183R7 |
Ligands and binding sites
- ZN · Zinc ion · metal · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 661 | 0.71 | 0.79 | 58 | empty |
| 2 | 291 | 0.58 | 0.77 | 34 | ZN |
| 3 | 103 | 0.39 | 0.76 | 22 | empty |
Interfaces
1 interface between chains.
- A–B · 429 Ų buried · 5 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 5A0P · PDBe 5A0P · UniProt Q183R7
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