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A structural characterization of POLY(ASPARTIC acid) hydrolase-1 from sphingomonas sp. kt-1.
Analyse A structural characterization of POLY(ASPARTIC acid) hydrolase-1 from… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6VE6
- Type
- protein
- Length
- 1,062 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- POLY(ASPARTIC acid) hydrolase-1
- UniProt
- Q7WSC1
- Pockets
- 10 · best druggability 0.73
Structure
x-ray diffraction · 2 distinct chains · 31% helix, 20% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, D | POLY(ASPARTIC acid) hydrolase-1 | protein | 266 | 31% helix, 20% strand | Q7WSC1 |
| C | POLY(ASPARTIC acid) hydrolase-1 | protein | 264 | 31% helix, 20% strand | Q7WSC1 |
Pockets
10 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 908 | 0.73 | 0.77 | 72 | empty |
| 2 | 809 | 0.73 | 0.78 | 78 | empty |
| 3 | 348 | 0.58 | 0.76 | 48 | empty |
| 4 | 168 | 0.48 | 0.76 | 33 | empty |
| 5 | 127 | 0.43 | 0.76 | 25 | empty |
Interfaces
5 interfaces between chains.
- C–D · 652 Ų buried · 7 hydrogen bonds · protein-protein
- A–B · 508 Ų buried · 1 hydrogen bond · protein-protein
- B–C · 282 Ų buried · 1 hydrogen bond · protein-protein
- A–D · 222 Ų buried · 1 hydrogen bond · protein-protein
- B–D · 74 Ų buried · 0 hydrogen bonds · protein-protein
Compared structures
- 6VE6 · A structural characterization of poly(aspartic acid) hydrolase-1 from Sphingomonas sp.… · the same entry in another collection · 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 Q7WSC1
- Elsewhere: RCSB PDB 6VE6 · PDBe 6VE6 · UniProt Q7WSC1
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