Research workbench
Three dimensional structure of human carbonic anhydrase XII in complex with benzenesulfonamide
Analyse Three dimensional structure of human carbonic anhydrase XII in complex with… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6QNL
- Type
- protein
- Length
- 1,040 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- O43570
- Ligands
- J92, ZN
Structure
x-ray diffraction · 1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D | — | protein | 260 | — | O43570 |
Ligands and binding sites
- J92 · methyl 4-[(4-chloranyl-2-cyclohexylsulfanyl-5-sulfamoyl-phenyl)carbonylamino]butanoate · ligand · 4 copies · chains A, B, C, D
- ZN · Zinc ion · metal · 4 copies · chains A, B, C, D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 6QNL · Three dimensional structure of human carbonic anhydrase XII in complex with… · the same entry in another collection · chain D against D, TM-score 1.00
- O43570 · AlphaFold monomer V2.0 prediction for carbonic anhydrase 12 (O43570) · a predicted model of the same protein · chain A against A, TM-score 1.00
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 6QNL · PDBe 6QNL · UniProt O43570
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