MolNFT v1 · #61991 · protein
H. influenzae beta-carbonic anhydrase, variant Y181F
3E28 · Carbonic anhydrase 2: “H. influenzae beta-carbonic anhydrase, variant Y181F”. X-ray diffraction, 2 ligands (ZN, SO4), 19 pockets (best druggability 0.76). MolNFT v1 #61991 on GenesisL1: 3D structure, binding sites and pockets in…
- PDB
- 3E28
- Type
- protein
- Length
- 1,232 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
- 19 · best druggability 0.76
Structure
x-ray diffraction · 6 distinct chains · 51% helix, 16% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Carbonic anhydrase 2 (EC 4.2.1.1) | protein | 215 | 51% helix, 15% strand | P45148 |
| B | Carbonic anhydrase 2 (EC 4.2.1.1) | protein | 206 | 50% helix, 16% strand | P45148 |
| C | Carbonic anhydrase 2 (EC 4.2.1.1) | protein | 204 | 52% helix, 15% strand | P45148 |
| D | Carbonic anhydrase 2 (EC 4.2.1.1) | protein | 201 | 52% helix, 18% strand | P45148 |
| E | Carbonic anhydrase 2 (EC 4.2.1.1) | protein | 202 | 50% helix, 15% strand | P45148 |
| F | Carbonic anhydrase 2 (EC 4.2.1.1) | protein | 204 | 52% helix, 18% strand | P45148 |
Ligands and binding sites
- ZN · Zinc ion · metal · 6 copies · chains A, B, C, D, E, F
- SO4 · Sulfate ion · ion · 16 copies · chains A, B, C, D, E, F
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
19 pockets found on a 1 Å grid, 8 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 93 | 0.76 | 0.97 | 36 | SO4 |
| 2 | 436 | 0.74 | 0.84 | 65 | SO4 |
| 3 | 303 | 0.74 | 0.87 | 45 | SO4 |
| 4 | 56 | 0.73 | 0.99 | 24 | empty |
| 5 | 308 | 0.73 | 0.86 | 46 | SO4 |
Interfaces
8 interfaces between chains.
- D–F · 2992 Ų buried · 32 hydrogen bonds · protein-protein
- C–E · 2836 Ų buried · 27 hydrogen bonds · protein-protein
- C–D · 997 Ų buried · 17 hydrogen bonds · protein-protein
- A–B · 957 Ų buried · 12 hydrogen bonds · protein-protein
- E–F · 953 Ų buried · 11 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 3E28 · PDBe 3E28 · UniProt P45148
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