Research workbench
Complex of double mutant (T89V,K162T) of E. COLI L-asparaginase II with L-asp
Analyse Complex of double mutant (T89V,K162T) of E. COLI L-asparaginase II with L-asp in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6V27
- Type
- protein
- Length
- 1,270 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- L-asparaginase 2
- EC
- 3.5.1.1
- UniProt
- P00805
- Pockets
- 12 · best druggability 0.63
Structure
x-ray diffraction · 3 distinct chains · 32% helix, 24% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, C | L-asparaginase 2 (EC 3.5.1.1) | protein | 326 | 33% helix, 24% strand | P00805 |
| B | L-asparaginase 2 (EC 3.5.1.1) | protein | 303 | 31% helix, 25% strand | P00805 |
| D | L-asparaginase 2 (EC 3.5.1.1) | protein | 315 | 33% helix, 23% strand | P00805 |
Pockets
12 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 126 | 0.63 | 0.87 | 29 | empty |
| 2 | 315 | 0.54 | 0.75 | 49 | empty |
| 3 | 95 | 0.54 | 0.84 | 23 | empty |
| 4 | 105 | 0.49 | 0.81 | 23 | empty |
| 5 | 88 | 0.46 | 0.81 | 21 | empty |
Interfaces
3 interfaces between chains.
- C–D · 2325 Ų buried · 53 hydrogen bonds · protein-protein
- A–B · 2313 Ų buried · 56 hydrogen bonds · protein-protein
- A–C · 232 Ų buried · 4 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 4 disulfide, 4 modified (disulfide, nonstandard).
Compared structures
- 6V27 · Complex of double mutant (T89V,K162T) of E. coli L-asparaginase II with L-Asp · the same entry in another collection · chain D against D, TM-score 1.00
- P00805 · AlphaFold monomer V2.0 prediction for L-asparaginase 2 (P00805) · a predicted model of the same protein · chain D 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 P00805
- Elsewhere: RCSB PDB 6V27 · PDBe 6V27 · UniProt P00805
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