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The crystal structure of the neisserial esterase D.
Analyse The crystal structure of the neisserial esterase D. in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4B6G
- Type
- protein
- Length
- 558 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Putative esterase
- EC
- 3.1.2.12
- UniProt
- Q9JZ43
- Pockets
- 2 · best druggability 0.60
Structure
x-ray diffraction · 2 distinct chains · 39% helix, 25% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Putative esterase (EC 3.1.2.12) | protein | 283 | 38% helix, 25% strand | Q9JZ43 |
| B | Putative esterase (EC 3.1.2.12) | protein | 275 | 39% helix, 24% strand | Q9JZ43 |
Pockets
2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 301 | 0.60 | 0.78 | 60 | empty |
| 2 | 62 | 0.30 | 0.74 | 20 | empty |
Interfaces
1 interface between chains.
- A–B · 947 Ų buried · 9 hydrogen bonds · protein-protein
Compared structures
- 4B6G · The Crystal Structure of the Neisserial Esterase D. · 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 Q9JZ43
- Elsewhere: RCSB PDB 4B6G · PDBe 4B6G · UniProt Q9JZ43
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