Research workbench
The crystal structure of kanj in complex with N-oxalylglycine
Analyse The crystal structure of kanj in complex with N-oxalylglycine in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7CL4
- Type
- protein
- Length
- 1,681 residues
- Chains
- 6
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- Q6L732
- Ligands
- OGA, NI
Structure
x-ray diffraction · 6 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 274 | — | Q6L732 |
| B | — | protein | 283 | — | Q6L732 |
| C | — | protein | 277 | — | Q6L732 |
| D | — | protein | 284 | — | Q6L732 |
| E | — | protein | 278 | — | Q6L732 |
| F | — | protein | 285 | — | Q6L732 |
Ligands and binding sites
- OGA · N-oxalylglycine · ligand · 6 copies · chains A, B, C, D, E, F
- NI · Nickel (II) ion · metal · 6 copies · chains A, B, C, D, E, F
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- Q6L732 · AlphaFold monomer V2.0 prediction for kanamycin B dioxygenase (Q6L732) · a predicted model of the same protein · chain A against A, TM-score 0.98
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 Q6L732
- Elsewhere: RCSB PDB 7CL4 · PDBe 7CL4 · UniProt Q6L732
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