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Carbonic anhydrase CAH3 from chlamydomonas reinhardtii in complex with phosphate.
Analyse Carbonic anhydrase CAH3 from chlamydomonas reinhardtii in complex with… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4XIX
- Type
- protein
- Length
- 1,904 residues
- Chains
- 8
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Carbonic anhydrase, alpha type
- UniProt
- Q39588
- Ligands
- ZN, 2HP
- Pockets
- 20 · best druggability 0.85
Structure
x-ray diffraction · 3 distinct chains · 13% helix, 33% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, E, F, G | Carbonic anhydrase, alpha type | protein | 238 | 13% helix, 32% strand | Q39588 |
| B, D | Carbonic anhydrase, alpha type | protein | 237 | 13% helix, 33% strand | Q39588 |
| C, H | Carbonic anhydrase, alpha type | protein | 239 | 13% helix, 33% strand | Q39588 |
Ligands and binding sites
- ZN · Zinc ion · metal · 8 copies · chains A, B, C, D, E, F, G, H
- 2HP · Dihydrogenphosphate ion · ion · 24 copies · chains A, G, B, H, C, E, D, 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, 12 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 945 | 0.85 | 0.86 | 91 | 2HP |
| 2 | 1035 | 0.83 | 0.84 | 112 | 2HP |
| 3 | 510 | 0.76 | 0.84 | 79 | 2HP |
| 4 | 513 | 0.70 | 0.80 | 73 | empty |
| 5 | 217 | 0.59 | 0.80 | 35 | empty |
Interfaces
13 interfaces between chains.
- C–E · 1654 Ų buried · 17 hydrogen bonds · protein-protein
- B–H · 1623 Ų buried · 18 hydrogen bonds · protein-protein
- A–G · 1565 Ų buried · 14 hydrogen bonds · protein-protein
- D–F · 1559 Ų buried · 16 hydrogen bonds · protein-protein
- B–C · 762 Ų buried · 3 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 8 disulfide (disulfide).
Compared structures
- 4XIX · Carbonic anhydrase Cah3 from Chlamydomonas reinhardtii in complex with phosphate. · the same entry in another collection · chain A against A, 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 Q39588
- Elsewhere: RCSB PDB 4XIX · PDBe 4XIX · UniProt Q39588
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