MolNFT v1 · #125846 · protein
Crystal structure of human carbonic anhydrase isozyme XII with 4-(1H- benzimidazol-1-ylacetyl)-2-chlorobenzenesulfonamide
5LL9 · Carbonic anhydrase 12: “Crystal structure of human carbonic anhydrase isozyme XII with 4-(1H…”. X-ray diffraction, 3 ligands (6YQ, ZN, SO4), 11 pockets (best druggability 0.82). MolNFT v1 #125846 on GenesisL1: 3D structure, binding…
- PDB
- 5LL9
- Type
- protein
- Length
- 1,044 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Carbonic anhydrase 12
- EC
- 4.2.1.1
- UniProt
- O43570
- Ligands
- 6YQ, ZN, SO4
- Pockets
- 11 · best druggability 0.82
Structure
x-ray diffraction · 1 distinct chain · 16% helix, 32% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D | Carbonic anhydrase 12 (EC 4.2.1.1) | protein | 261 | 16% helix, 32% strand | O43570 |
Ligands and binding sites
- 6YQ · 4-[2-(benzimidazol-1-yl)ethanoyl]-2-chloranyl-benzenesulfonamide · ligand · 4 copies · chains A, B, C, D
- ZN · Zinc ion · metal · 4 copies · chains A, B, C, D
- SO4 · Sulfate ion · ion · 3 copies · chains B, C, D
- EDO · 1,2-ethanediol · additive · 11 copies · chains A, B, C, D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
11 pockets found on a 1 Å grid, 8 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1159 | 0.82 | 0.84 | 116 | EDO |
| 2 | 1020 | 0.80 | 0.82 | 122 | EDO |
| 3 | 229 | 0.74 | 0.89 | 39 | empty |
| 4 | 82 | 0.71 | 0.96 | 25 | empty |
| 5 | 220 | 0.59 | 0.80 | 30 | 6YQ, EDO |
Interfaces
5 interfaces between chains.
- A–B · 1153 Ų buried · 27 hydrogen bonds · protein-protein
- C–D · 1148 Ų buried · 26 hydrogen bonds · protein-protein
- B–D · 480 Ų buried · 4 hydrogen bonds · protein-protein
- A–C · 364 Ų buried · 3 hydrogen bonds · protein-protein
- A–D · 12 Ų buried · 0 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 4 disulfide (disulfide).
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 O43570
- Elsewhere: RCSB PDB 5LL9 · PDBe 5LL9 · UniProt O43570
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