Research workbench
Structural basis for domain rotation during adenylation of active site K123 and fragment library screening against NAD+ -dependent DNA ligase from mycobacterium tuberculosis
Analyse Structural basis for domain rotation during adenylation of active site K123 and… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6KJM
- Type
- protein
- Length
- 321 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P9WNV1
- Ligands
- NMN, AMP, SO4
Structure
x-ray diffraction · 1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 321 | — | P9WNV1 |
Ligands and binding sites
- NMN · Beta-nicotinamide ribose monophosphate · ligand · chains A
- AMP · Adenosine monophosphate · ligand · chains A
- SO4 · Sulfate ion · ion · 4 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 6KJM · Structural basis for domain rotation during adenylation of active site K123 and fragment… · the same entry in another collection · chain A against A, TM-score 1.00
- P9WNV1 · AlphaFold monomer V2.0 prediction for DNA ligase a (P9WNV1) · 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 P9WNV1
- Elsewhere: RCSB PDB 6KJM · PDBe 6KJM · UniProt P9WNV1
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