Research workbench
Human carbonic anhydrase XII bound by 3,5-diphenylbenzenesulfonamide
Analyse Human carbonic anhydrase XII bound by 3,5-diphenylbenzenesulfonamide in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6T5Q
- Type
- protein
- Length
- 1,042 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- O43570
- Ligands
- MKQ, ZN
Structure
x-ray diffraction · 2 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, D | — | protein | 260 | — | O43570 |
| B, C | — | protein | 261 | — | O43570 |
Ligands and binding sites
- MKQ · 3,5-diphenylbenzenesulfonamide · ligand · 3 copies · chains A, B, C
- ZN · Zinc ion · metal · 4 copies · chains A, B, C, D
- EDO · 1,2-ethanediol · additive · 2 copies · chains B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 6T5Q · Human Carbonic anhydrase XII bound by 3,5-diphenylbenzenesulfonamide · 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 6T5Q · PDBe 6T5Q · UniProt O43570
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