Research workbench
Crystal structure of MET260ALA mutant of E. COLI aminopeptidase N in complex with L-glutamate
Analyse Crystal structure of MET260ALA mutant of E. COLI aminopeptidase N in complex… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4XN1
- Type
- protein
- Length
- 867 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
- GLU, NA, ZN
- Pockets
- 8 · best druggability 0.82
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 | 867 | 45% helix, 22% strand | P04825 |
Ligands and binding sites
- GLU · Glutamic acid · ligand · chains A
- NA · Sodium ion · metal · 10 copies · chains A
- ZN · Zinc ion · metal · chains A
- MLI · Malonate ion · additive · 3 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
8 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 502 | 0.82 | 0.89 | 82 | GLU, NA |
| 2 | 482 | 0.79 | 0.86 | 60 | MLI |
| 3 | 235 | 0.72 | 0.87 | 37 | empty |
| 4 | 616 | 0.69 | 0.78 | 62 | NA |
| 5 | 151 | 0.45 | 0.76 | 24 | empty |
Compared structures
- 4XN1 · Crystal Structure of Met260Ala mutant of E. coli Aminopeptidase N in complex with… · the same entry in another collection · chain A against A, TM-score 1.00
- P04825 · AlphaFold monomer V2.0 prediction for aminopeptidase N (P04825) · 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 P04825
- Elsewhere: RCSB PDB 4XN1 · PDBe 4XN1 · UniProt P04825
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