Research workbench
Crystal structure of mouse carnosinase CN2 complexed with mn and bestatin
Analyse Crystal structure of mouse carnosinase CN2 complexed with mn and bestatin in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2ZOF
- Type
- protein
- Length
- 956 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Cytosolic non-specific dipeptidase
- EC
- 3.4.13.18
- UniProt
- Q9D1A2
- Ligands
- BES, MN
- Pockets
- 9 · best druggability 0.69
Structure
x-ray diffraction · 1 distinct chain · 36% helix, 23% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Cytosolic non-specific dipeptidase (EC 3.4.13.18) | protein | 478 | 36% helix, 23% strand | Q9D1A2 |
Ligands and binding sites
- BES · 2-(3-amino-2-hydroxy-4-phenyl-butyrylamino)-4-methyl-pentanoic acid · ligand · 2 copies · chains A, B
- MN · Manganese (II) ion · metal · 4 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
9 pockets found on a 1 Å grid, 6 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 411 | 0.69 | 0.81 | 60 | MN, BES |
| 2 | 190 | 0.69 | 0.87 | 39 | MN, BES |
| 3 | 127 | 0.67 | 0.89 | 33 | empty |
| 4 | 433 | 0.63 | 0.77 | 57 | empty |
| 5 | 101 | 0.58 | 0.86 | 26 | empty |
Interfaces
1 interface between chains.
- A–B · 3701 Ų buried · 55 hydrogen bonds · protein-protein
Compared structures
- 2ZOF · Crystal structure of mouse carnosinase CN2 complexed with MN and bestatin · the same entry in another collection · chain A against A, TM-score 1.00
- Q9D1A2 · AlphaFold monomer V2.0 prediction for cytosolic non-specific dipeptidase (Q9D1A2) · a predicted model of the same protein · chain A against A, TM-score 0.95
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 Q9D1A2
- Elsewhere: RCSB PDB 2ZOF · PDBe 2ZOF · UniProt Q9D1A2
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