MolNFT v2 · #155766 · protein
Structural basis for domain rotation during adenylation of active site K123 and fragment library screening against NAD+ -dependent DNA ligase from Mycobacterium tuberculosis
6KKV: “Structural basis for domain rotation during adenylation of active site K123 and fragment library screening…”. X-ray diffraction at 2.56, 2 ligands (DKR, SO4). MolNFT v2 #155766 on GenesisL1: 3D structure, binding sites and pockets…
- PDB
- 6KKV
- Type
- protein
- Length
- 321 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 2.56
- Source
- Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
- UniProt
- P9WNV1
- Ligands
- DKR, SO4
Structure
x-ray diffraction · resolution 2.56 · 1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 321 | — | P9WNV1 |
Ligands and binding sites
- DKR · N-[(4-methylphenyl)methyl]-1H-pyrrole-2-carboxamide · ligand · chains A
- SO4 · Sulfate ion · ion · 2 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 6KKV · 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 6KKV · PDBe 6KKV · UniProt P9WNV1
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