Research workbench
Crystal structure of cold-active esterase PMGL3 from permafrost metagenomic library
Analyse Crystal structure of cold-active esterase PMGL3 from permafrost metagenomic… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7B1X
- Type
- protein
- Length
- 604 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Esterase PMGL3
- EC
- 3.1.1.3
- Pockets
- 4 · best druggability 0.75
Structure
x-ray diffraction · 1 distinct chain · 45% helix, 19% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Esterase PMGL3 (EC 3.1.1.3) | protein | 302 | 45% helix, 19% strand | — |
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 | 447 | 0.75 | 0.84 | 43 | empty |
| 2 | 463 | 0.75 | 0.83 | 40 | empty |
| 3 | 273 | 0.54 | 0.76 | 31 | empty |
| 4 | 147 | 0.40 | 0.73 | 24 | empty |
Interfaces
1 interface between chains.
- A–B · 958 Ų buried · 20 hydrogen bonds · protein-protein
Compared structures
- 7B1X · Crystal structure of cold-active esterase PMGL3 from permafrost metagenomic library · 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
- Elsewhere: RCSB PDB 7B1X · PDBe 7B1X
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