MolNFT v1 · #34759 · protein
Crystal structure of aminopeptidase N from escherichia COLI
2DQ6: “Crystal structure of aminopeptidase N from escherichia COLI”. X-ray diffraction, 2 ligands (ZN, SO4), 12 pockets (best druggability 0.80). MolNFT v1 #34759 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 2DQ6
- Type
- protein
- Length
- 865 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Aminopeptidase N
- EC
- 3.4.11.2
- UniProt
- P04825
- Ligands
- ZN, SO4
- Pockets
- 12 · best druggability 0.80
Structure
x-ray diffraction · 1 distinct chain · 45% helix, 22% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Aminopeptidase N (EC 3.4.11.2) | protein | 865 | 45% helix, 22% strand | P04825 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
12 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 420 | 0.80 | 0.88 | 64 | SO4 |
| 2 | 514 | 0.74 | 0.82 | 58 | empty |
| 3 | 242 | 0.71 | 0.86 | 36 | empty |
| 4 | 193 | 0.68 | 0.86 | 31 | empty |
| 5 | 514 | 0.67 | 0.78 | 56 | empty |
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 P04825
- Elsewhere: RCSB PDB 2DQ6 · PDBe 2DQ6 · UniProt P04825
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.