Research workbench
ATP sulfurylase from S. cerevisiae
Analyse ATP sulfurylase from S. cerevisiae in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1G8F
- Type
- protein
- Length
- 510 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Sulfate adenylyltransferase
- EC
- 2.7.7.4
- UniProt
- P08536
- Ligands
- CD, CA, NA, MG, SO4
- Pockets
- 6 · best druggability 0.69
Structure
x-ray diffraction · 1 distinct chain · 38% helix, 18% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Sulfate adenylyltransferase (EC 2.7.7.4) | protein | 510 | 38% helix, 18% strand | P08536 |
Ligands and binding sites
- CD · Cadmium ion · metal · 5 copies · chains A
- CA · Calcium ion · metal · 3 copies · chains A
- NA · Sodium ion · metal · 2 copies · chains A
- MG · Magnesium ion · metal · chains A
- SO4 · Sulfate ion · ion · 2 copies · chains A
- ACY · Acetic acid · additive · 11 copies · chains A
- TRS · 2-amino-2-hydroxymethyl-propane-1,3-diol · additive · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
6 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 532 | 0.69 | 0.78 | 46 | SO4 |
| 2 | 50 | 0.36 | 0.79 | 12 | empty |
| 3 | 82 | 0.35 | 0.76 | 16 | CD, SO4 |
| 4 | 68 | 0.32 | 0.75 | 12 | empty |
| 5 | 56 | 0.27 | 0.74 | 11 | empty |
Compared structures
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 P08536
- Elsewhere: RCSB PDB 1G8F · PDBe 1G8F · UniProt P08536
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