MolNFT v1 · #158542 · protein
ECAII(D90T,K162T) mutant in complex with citrate at pH 5.6
6NX7 · L-asparaginase 2: “ECAII(D90T,K162T) mutant in complex with citrate at pH 5.6”. X-ray diffraction, 6 pockets (best druggability 0.48). MolNFT v1 #158542 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 6NX7
- Type
- protein
- Length
- 624 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- L-asparaginase 2
- EC
- 3.5.1.1
- UniProt
- P00805
- Pockets
- 6 · best druggability 0.48
Structure
x-ray diffraction · 1 distinct chain · 34% helix, 21% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | L-asparaginase 2 (EC 3.5.1.1) | protein | 312 | 34% helix, 21% strand | P00805 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
6 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 134 | 0.48 | 0.79 | 20 | empty |
| 2 | 173 | 0.48 | 0.76 | 31 | empty |
| 3 | 115 | 0.46 | 0.79 | 20 | empty |
| 4 | 62 | 0.29 | 0.75 | 18 | CIT |
| 5 | 60 | 0.28 | 0.74 | 19 | ACY |
Interfaces
1 interface between chains.
- A–B · 991 Ų buried · 15 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 2 disulfide (disulfide).
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 P00805
- Elsewhere: RCSB PDB 6NX7 · PDBe 6NX7 · UniProt P00805
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