MolNFT v1 · #127290 · protein
Crystal structure of human carbonic anhydrase isozyme XII with 2,3,5, 6-tetrafluoro-4[(2-HYDROXYETHYL)SULFONYL]BENZENESULFONAMIDE
5MSB · Carbonic anhydrase 12: “Crystal structure of human carbonic anhydrase isozyme XII with 2,3,5…”. X-ray diffraction, 2 ligands (V13, ZN), 9 pockets (best druggability 0.85). MolNFT v1 #127290 on GenesisL1: 3D structure, binding sites…
- PDB
- 5MSB
- Type
- protein
- Length
- 1,043 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
- V13, ZN
- Pockets
- 9 · best druggability 0.85
Structure
x-ray diffraction · 2 distinct chains · 17% helix, 31% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C | Carbonic anhydrase 12 (EC 4.2.1.1) | protein | 261 | 17% helix, 31% strand | O43570 |
| D | Carbonic anhydrase 12 (EC 4.2.1.1) | protein | 260 | 16% helix, 32% strand | O43570 |
Ligands and binding sites
- V13 · 2,3,5,6-tetrafluoro-4-[(2-hydroxyethyl) sulfonyl]benzenesulfonamide · ligand · 4 copies · chains A, B, C, D
- ZN · Zinc ion · metal · 4 copies · chains A, B, C, D
- EDO · 1,2-ethanediol · additive · 6 copies · chains A, B, D
- PEG · Di(hydroxyethyl)ether · additive · chains B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
9 pockets found on a 1 Å grid, 7 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1090 | 0.85 | 0.86 | 127 | EDO |
| 2 | 965 | 0.83 | 0.84 | 106 | empty |
| 3 | 682 | 0.67 | 0.76 | 62 | empty |
| 4 | 225 | 0.60 | 0.80 | 26 | V13 |
| 5 | 219 | 0.60 | 0.81 | 28 | V13 |
Interfaces
4 interfaces between chains.
- A–B · 1190 Ų buried · 28 hydrogen bonds · protein-protein
- C–D · 1133 Ų buried · 29 hydrogen bonds · protein-protein
- B–D · 476 Ų buried · 4 hydrogen bonds · protein-protein
- A–C · 286 Ų buried · 4 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 5MSB · PDBe 5MSB · UniProt O43570
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