Research workbench
H. influenzae beta-carbonic anhydrase, variant G41A with 100 mm bicarbonate
Analyse H. influenzae beta-carbonic anhydrase, variant G41A with 100 mm bicarbonate in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3E3I
- Type
- protein
- Length
- 2,514 residues
- Chains
- 12
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Carbonic anhydrase 2
- EC
- 4.2.1.1
- UniProt
- P45148
- Ligands
- BCT, ZN, SO4
- Pockets
- 20 · best druggability 0.78
Structure
x-ray diffraction · 9 distinct chains · 52% helix, 16% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, C | Carbonic anhydrase 2 (EC 4.2.1.1) | protein | 208 | 51% helix, 17% strand | P45148 |
| B, E | Carbonic anhydrase 2 (EC 4.2.1.1) | protein | 212 | 51% helix, 16% strand | P45148 |
| D | Carbonic anhydrase 2 (EC 4.2.1.1) | protein | 213 | 51% helix, 14% strand | P45148 |
| F | Carbonic anhydrase 2 (EC 4.2.1.1) | protein | 208 | 52% helix, 16% strand | P45148 |
| G | Carbonic anhydrase 2 (EC 4.2.1.1) | protein | 214 | 52% helix, 17% strand | P45148 |
| H, K | Carbonic anhydrase 2 (EC 4.2.1.1) | protein | 209 | 52% helix, 16% strand | P45148 |
| I | Carbonic anhydrase 2 (EC 4.2.1.1) | protein | 210 | 52% helix, 16% strand | P45148 |
| J | Carbonic anhydrase 2 (EC 4.2.1.1) | protein | 205 | 53% helix, 17% strand | P45148 |
| L | Carbonic anhydrase 2 (EC 4.2.1.1) | protein | 206 | 53% helix, 17% strand | P45148 |
Ligands and binding sites
- BCT · Bicarbonate ion · ligand · 11 copies · chains B, A, C, D, E, F, G, H, I, J, K, L
- ZN · Zinc ion · metal · 12 copies · chains A, B, C, D, E, F, G, H, I, J, K, L
- SO4 · Sulfate ion · ion · 13 copies · chains A, B, C, D, E, F, G, H, I, J, K, L
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
20 pockets found on a 1 Å grid, 18 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1082 | 0.78 | 0.80 | 57 | empty |
| 2 | 425 | 0.77 | 0.86 | 67 | SO4 |
| 3 | 479 | 0.77 | 0.85 | 60 | SO4 |
| 4 | 415 | 0.76 | 0.85 | 52 | SO4 |
| 5 | 347 | 0.76 | 0.87 | 45 | SO4 |
Interfaces
27 interfaces between chains.
- E–G · 3188 Ų buried · 34 hydrogen bonds · protein-protein
- B–D · 3122 Ų buried · 34 hydrogen bonds · protein-protein
- F–H · 3104 Ų buried · 33 hydrogen bonds · protein-protein
- A–C · 3045 Ų buried · 33 hydrogen bonds · protein-protein
- J–L · 3028 Ų buried · 35 hydrogen bonds · protein-protein
Compared structures
- 3E3I · H. influenzae beta-carbonic anhydrase, variant G41A with 100 mM bicarbonate · the same entry in another collection · chain L against L, 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 P45148
- Elsewhere: RCSB PDB 3E3I · PDBe 3E3I · UniProt P45148
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