Research workbench
Biochemical characterization and structural analysis of a new cold- active and salt tolerant esterase from the marine bacterium thalassospira sp
Analyse Biochemical characterization and structural analysis of a new cold- active and… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4V2I
- Type
- protein
- Length
- 630 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- ESTERASE/LIPASE
- EC
- 3.1.1.1
- UniProt
- A0A023T3X2
- Ligands
- MG
- Pockets
- 4 · best druggability 0.64
Structure
x-ray diffraction · 1 distinct chain · 42% helix, 20% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | ESTERASE/LIPASE (EC 3.1.1.1) | protein | 315 | 42% helix, 20% strand | A0A023T3X2 |
Ligands and binding sites
- MG · Magnesium ion · metal · 3 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
4 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 264 | 0.64 | 0.81 | 38 | empty |
| 2 | 280 | 0.64 | 0.80 | 39 | empty |
| 3 | 180 | 0.52 | 0.78 | 28 | empty |
| 4 | 155 | 0.49 | 0.78 | 28 | empty |
Interfaces
1 interface between chains.
- A–B · 1026 Ų buried · 15 hydrogen bonds · protein-protein
Compared structures
- 4V2I · Biochemical characterization and structural analysis of a new cold- active and salt… · 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 A0A023T3X2
- Elsewhere: RCSB PDB 4V2I · PDBe 4V2I · UniProt A0A023T3X2
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