Research workbench
H. influenzae beta-carbonic anhydrase variant W39V/G41A/P48S/A49P
Analyse H. influenzae beta-carbonic anhydrase variant W39V/G41A/P48S/A49P in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4WAM
- Type
- protein
- Length
- 358 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Beta-carbonic anhydrase
- EC
- 4.2.1.1
- UniProt
- P45148
- Ligands
- ZN, PO4
- Pockets
- 4 · best druggability 0.76
Structure
x-ray diffraction · 2 distinct chains · 48% helix, 18% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Beta-carbonic anhydrase (EC 4.2.1.1) | protein | 178 | 48% helix, 16% strand | P45148 |
| B | Beta-carbonic anhydrase (EC 4.2.1.1) | protein | 180 | 48% helix, 20% strand | P45148 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
4 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 328 | 0.76 | 0.88 | 48 | PO4 |
| 2 | 71 | 0.38 | 0.78 | 14 | empty |
| 3 | 72 | 0.34 | 0.75 | 13 | empty |
| 4 | 68 | 0.32 | 0.75 | 17 | PO4 |
Interfaces
1 interface between chains.
- A–B · 963 Ų buried · 19 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 4WAM · PDBe 4WAM · UniProt P45148
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