MolNFT v1 · #59547 · protein
Hexagonal crystal structure of precursor E. COLI isoaspartyl PEPTIDASE/L-asparaginase (ecaiii) with active-site T179A mutation
3C17 · L-asparaginase precursor: “Hexagonal crystal structure of precursor E. COLI isoaspartyl PEPTIDASE/L-asparaginase (ecaiii) with…”. X-ray diffraction, 2 ligands (NA, CL), 3 pockets (best druggability 0.49). MolNFT v1 #59547 on…
- PDB
- 3C17
- Type
- protein
- Length
- 611 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- L-asparaginase precursor
- EC
- 3.4.19.5, 3.5.1.1
- UniProt
- P37595
- Ligands
- NA, CL
- Pockets
- 3 · best druggability 0.49
Structure
x-ray diffraction · 2 distinct chains · 35% helix, 26% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | L-asparaginase precursor (EC 3.4.19.5, 3.5.1.1) | protein | 305 | 35% helix, 26% strand | P37595 |
| B | L-asparaginase precursor (EC 3.4.19.5, 3.5.1.1) | protein | 306 | 35% helix, 26% strand | P37595 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 197 | 0.49 | 0.76 | 28 | empty |
| 2 | 57 | 0.39 | 0.80 | 19 | NA |
| 3 | 50 | 0.26 | 0.74 | 16 | empty |
Interfaces
1 interface between chains.
- A–B · 1586 Ų buried · 18 hydrogen bonds · protein-protein
Compared structures
- 3C17 · Hexagonal Crystal Structure of Precursor E. coli Isoaspartyl Peptidase/l-Asparaginase… · the same entry in another collection · chain B against B, TM-score 1.00
- P37595 · AlphaFold monomer V2.0 prediction for isoaspartyl peptidase (P37595) · 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 P37595
- Elsewhere: RCSB PDB 3C17 · PDBe 3C17 · UniProt P37595
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