Research workbench
Sad phasing on nickel-substituted human carbonic anhydrase II
Analyse Sad phasing on nickel-substituted human carbonic anhydrase II in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6H6S
- Type
- protein
- Length
- 516 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Carbonic anhydrase 2
- EC
- 4.2.1.1
- UniProt
- P00918
- Ligands
- NI
- Pockets
- 8 · best druggability 0.60
Structure
x-ray diffraction · 1 distinct chain · 15% helix, 30% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Carbonic anhydrase 2 (EC 4.2.1.1) | protein | 258 | 15% helix, 30% strand | P00918 |
Ligands and binding sites
- NI · Nickel (II) ion · metal · 4 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
8 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 197 | 0.60 | 0.81 | 26 | empty |
| 2 | 172 | 0.59 | 0.82 | 29 | empty |
| 3 | 114 | 0.48 | 0.80 | 26 | empty |
| 4 | 67 | 0.31 | 0.75 | 14 | empty |
| 5 | 62 | 0.30 | 0.75 | 13 | empty |
Interfaces
1 interface between chains.
- A–B · 395 Ų buried · 6 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 P00918
- Elsewhere: RCSB PDB 6H6S · PDBe 6H6S · UniProt P00918
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