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The structure of the beta-carbonic anhydrase ccaa
Analyse The structure of the beta-carbonic anhydrase ccaa in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5SWC
- Type
- protein
- Length
- 1,296 residues
- Chains
- 6
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Carbonic anhydrase
- EC
- 4.2.1.1
- UniProt
- Q54735
- Ligands
- ZN, CL
- Pockets
- 20 · best druggability 0.77
Structure
x-ray diffraction · 4 distinct chains · 48% helix, 17% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, E | Carbonic anhydrase (EC 4.2.1.1) | protein | 223 | 47% helix, 16% strand | Q54735 |
| C | Carbonic anhydrase (EC 4.2.1.1) | protein | 208 | 51% helix, 17% strand | Q54735 |
| D | Carbonic anhydrase (EC 4.2.1.1) | protein | 206 | 49% helix, 17% strand | Q54735 |
| F | Carbonic anhydrase (EC 4.2.1.1) | protein | 213 | 48% helix, 17% strand | Q54735 |
Ligands and binding sites
- ZN · Zinc ion · metal · 6 copies · chains A, B, C, D, E, F
- CL · Chloride ion · ion · 5 copies · chains A, B, C, D, E, F
- FMT · Formic acid · additive · 21 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, 6 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 649 | 0.77 | 0.83 | 99 | FMT |
| 2 | 305 | 0.69 | 0.83 | 58 | FMT |
| 3 | 415 | 0.65 | 0.78 | 69 | CL |
| 4 | 221 | 0.62 | 0.82 | 35 | FMT |
| 5 | 227 | 0.59 | 0.80 | 37 | empty |
Interfaces
12 interfaces between chains.
- E–F · 3800 Ų buried · 56 hydrogen bonds · protein-protein
- A–B · 3605 Ų buried · 43 hydrogen bonds · protein-protein
- C–D · 3527 Ų buried · 45 hydrogen bonds · protein-protein
- B–C · 1556 Ų buried · 18 hydrogen bonds · protein-protein
- D–E · 1547 Ų buried · 16 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 Q54735
- Elsewhere: RCSB PDB 5SWC · PDBe 5SWC · UniProt Q54735
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