Research workbench
Npsa-thda, an artificially fused adenylation-pcp di-domain nrps from klebsiella oxytoca
Analyse Npsa-thda, an artificially fused adenylation-pcp di-domain nrps from klebsiella… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6VHY
- Type
- protein
- Length
- 2,093 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- A0A2U4DY99, A0A2U4DNX7
- Ligands
- QXD
Structure
x-ray diffraction · 4 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 527 | — | A0A2U4DY99, A0A2U4DNX7 |
| B | — | protein | 527 | — | A0A2U4DY99, A0A2U4DNX7 |
| C | — | protein | 540 | — | A0A2U4DY99, A0A2U4DNX7 |
| D | — | protein | 499 | — | A0A2U4DY99, A0A2U4DNX7 |
Ligands and binding sites
- QXD · 5'-deoxy-5'-({[(2R)-2-{[2-({N-[(2R)-2-hydroxy-3,3-dimethyl-4-(phosphonooxy)butanoyl]-beta-alanyl}amino) ethyl]sulfanyl}-2-(3-hydroxyphenyl) ethyl]sulfonyl}amino)adenosine · ligand · 4 copies · chains A, C, B, D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 6VHY · NpsA-ThdA, an artificially fused Adenylation-PCP di-domain NRPS from Klebsiella oxytoca · the same entry in another collection · 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 A0A2U4DY99
- Every structure of UniProt A0A2U4DNX7
- Elsewhere: RCSB PDB 6VHY · PDBe 6VHY · UniProt A0A2U4DY99 · UniProt A0A2U4DNX7
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