Research workbench
Human carboanhydrase F131C_C206S double mutant in complex with sa-2
Analyse Human carboanhydrase F131C_C206S double mutant in complex with sa-2 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5T71
- Type
- protein
- Length
- 257 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Carbonic anhydrase 2
- EC
- 4.2.1.1
- UniProt
- P00918
- Ligands
- HGB, 75W, ZN
- Pockets
- 1 · best druggability 0.57
Structure
x-ray diffraction · 1 distinct chain · 15% helix, 31% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Carbonic anhydrase 2 (EC 4.2.1.1) | protein | 257 | 15% helix, 31% strand | P00918 |
Ligands and binding sites
- HGB · 4-(hydroxymercury)benzoic acid · ligand · chains A
- 75W · 4-[(E)-diazenyl]benzene-1-sulfonamide · ligand · chains A
- ZN · Zinc ion · metal · chains A
- TRS · 2-amino-2-hydroxymethyl-propane-1,3-diol · additive · 2 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 179 | 0.57 | 0.80 | 26 | HGB, 75W, TRS |
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 P00918
- Elsewhere: RCSB PDB 5T71 · PDBe 5T71 · UniProt P00918
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