Research workbench
Haemophilus influenzae beta-carbonic anhydrase
Analyse Haemophilus influenzae beta-carbonic anhydrase in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2A8C
- Type
- protein
- Length
- 1,315 residues
- Chains
- 6
- 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, SO4
- Pockets
- 20 · best druggability 0.77
Structure
x-ray diffraction · 4 distinct chains · 51% helix, 15% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Carbonic anhydrase 2 (EC 4.2.1.1) | protein | 221 | 52% helix, 16% strand | P45148 |
| C, F | Carbonic anhydrase 2 (EC 4.2.1.1) | protein | 219 | 50% helix, 14% strand | P45148 |
| D | Carbonic anhydrase 2 (EC 4.2.1.1) | protein | 215 | 52% helix, 16% strand | P45148 |
| E | Carbonic anhydrase 2 (EC 4.2.1.1) | protein | 220 | 49% helix, 13% strand | P45148 |
Ligands and binding sites
- ZN · Zinc ion · metal · 6 copies · chains A, B, C, D, E, F
- SO4 · Sulfate ion · ion · 6 copies · chains A, B, C, D, E, F
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
20 pockets found on a 1 Å grid, 8 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 380 | 0.77 | 0.87 | 49 | SO4 |
| 2 | 444 | 0.76 | 0.85 | 61 | SO4 |
| 3 | 287 | 0.75 | 0.87 | 35 | empty |
| 4 | 52 | 0.73 | 0.99 | 24 | empty |
| 5 | 171 | 0.54 | 0.79 | 31 | empty |
Interfaces
8 interfaces between chains.
- C–E · 3307 Ų buried · 34 hydrogen bonds · protein-protein
- D–F · 3298 Ų buried · 32 hydrogen bonds · protein-protein
- C–D · 984 Ų buried · 13 hydrogen bonds · protein-protein
- A–B · 967 Ų buried · 13 hydrogen bonds · protein-protein
- E–F · 929 Ų buried · 12 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 2A8C · PDBe 2A8C · UniProt P45148
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.