Research workbench
Structure of aminoadipate-semialdehyde dehydrogenase- phosphopantetheinyl transferase
Analyse Structure of aminoadipate-semialdehyde dehydrogenase- phosphopantetheinyl… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2BYD
- Type
- protein
- Length
- 283 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- HSPC223
- EC
- 1.2.1.31
- UniProt
- Q9P0Q3
- Ligands
- BR
- Pockets
- 4 · best druggability 0.53
Structure
x-ray diffraction · 1 distinct chain · 36% helix, 23% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | HSPC223 (EC 1.2.1.31) | protein | 283 | 36% helix, 23% strand | Q9P0Q3 |
Ligands and binding sites
- BR · Bromide ion · ion · 9 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
4 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 241 | 0.53 | 0.76 | 35 | BR |
| 2 | 183 | 0.51 | 0.77 | 31 | BR |
| 3 | 60 | 0.47 | 0.84 | 13 | empty |
| 4 | 51 | 0.27 | 0.74 | 14 | empty |
Compared structures
- 2BYD · Structure of aminoadipate-semialdehyde dehydrogenase- phosphopantetheinyl transferase · 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 Q9P0Q3
- Elsewhere: RCSB PDB 2BYD · PDBe 2BYD · UniProt Q9P0Q3
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