Research workbench
H. influenzae beta-carbonic anhydrase, variant V47A
Analyse H. influenzae beta-carbonic anhydrase, variant V47A in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3E31
- Type
- protein
- Length
- 364 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Carbonic anhydrase 2
- EC
- 4.2.1.1
- UniProt
- P45148
- Ligands
- ZN
- Pockets
- 3 · best druggability 0.48
Structure
x-ray diffraction · 2 distinct chains · 49% helix, 16% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Carbonic anhydrase 2 (EC 4.2.1.1) | protein | 183 | 49% helix, 16% strand | P45148 |
| B | Carbonic anhydrase 2 (EC 4.2.1.1) | protein | 181 | 48% helix, 17% strand | P45148 |
Ligands and binding sites
- ZN · Zinc ion · metal · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 100 | 0.48 | 0.81 | 25 | empty |
| 2 | 52 | 0.28 | 0.74 | 15 | empty |
| 3 | 52 | 0.26 | 0.74 | 17 | empty |
Interfaces
1 interface between chains.
- A–B · 1433 Ų buried · 17 hydrogen bonds · protein-protein
Compared structures
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 P45148
- Elsewhere: RCSB PDB 3E31 · PDBe 3E31 · UniProt P45148
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