Research workbench
ECAII(D90T,K162T) mutant in complex with citrate at pH 6.2
Analyse ECAII(D90T,K162T) mutant in complex with citrate at pH 6.2 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6NX8
- 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
- 4 · best druggability 0.60
Structure
x-ray diffraction · 2 distinct chains · 33% helix, 21% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | L-asparaginase 2 (EC 3.5.1.1) | protein | 313 | 33% helix, 21% strand | P00805 |
| B | L-asparaginase 2 (EC 3.5.1.1) | protein | 311 | 33% helix, 22% strand | P00805 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
4 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 340 | 0.60 | 0.77 | 52 | empty |
| 2 | 217 | 0.51 | 0.76 | 30 | empty |
| 3 | 57 | 0.30 | 0.76 | 18 | CIT |
| 4 | 62 | 0.29 | 0.75 | 19 | ACY |
Interfaces
1 interface between chains.
- A–B · 980 Ų buried · 16 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 6NX8 · PDBe 6NX8 · UniProt P00805
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