Research workbench
Crystal structure of mycobacterium abscessus phosphopantetheine adenylyltransferase in complex with fragment 9
Analyse Crystal structure of mycobacterium abscessus phosphopantetheine… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7YY5
- Type
- protein
- Length
- 469 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- B1MDL6
- Ligands
- I7L
Structure
x-ray diffraction · 3 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 158 | — | B1MDL6 |
| B | — | protein | 157 | — | B1MDL6 |
| C | — | protein | 154 | — | B1MDL6 |
Ligands and binding sites
- I7L · 2-naphthalen-2-ylethanoic acid · ligand · 2 copies · chains B, C
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 7YY5 · Crystal structure of Mycobacterium abscessus Phosphopantetheine adenylyltransferase in… · the same entry in another collection · chain A against A, TM-score 1.00
- B1MDL6 · AlphaFold monomer V2.0 prediction for phosphopantetheine adenylyltransferase (B1MDL6) · a predicted model of the same protein · chain C 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 B1MDL6
- Elsewhere: RCSB PDB 7YY5 · PDBe 7YY5 · UniProt B1MDL6
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