Research workbench
Crystal structure of mouse sulfotransferase SULT7A1 complexed with pap
Analyse Crystal structure of mouse sulfotransferase SULT7A1 complexed with pap in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5X2B
- Type
- protein
- Length
- 3,339 residues
- Chains
- 12
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Sulfotransferase
- EC
- 2.8.2.-
- UniProt
- B7ZWN4
- Ligands
- A3P, CA
- Pockets
- 20 · best druggability 0.87
Structure
x-ray diffraction · 10 distinct chains · 45% helix, 13% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| C | Sulfotransferase (EC 2.8.2.-) | protein | 282 | 45% helix, 12% strand | B7ZWN4 |
| A, K | Sulfotransferase (EC 2.8.2.-) | protein | 281 | 44% helix, 13% strand | B7ZWN4 |
| B | Sulfotransferase (EC 2.8.2.-) | protein | 275 | 45% helix, 13% strand | B7ZWN4 |
| D | Sulfotransferase (EC 2.8.2.-) | protein | 276 | 46% helix, 13% strand | B7ZWN4 |
| E, I | Sulfotransferase (EC 2.8.2.-) | protein | 277 | 46% helix, 13% strand | B7ZWN4 |
| F | Sulfotransferase (EC 2.8.2.-) | protein | 279 | 45% helix, 13% strand | B7ZWN4 |
| G | Sulfotransferase (EC 2.8.2.-) | protein | 276 | 47% helix, 13% strand | B7ZWN4 |
| H | Sulfotransferase (EC 2.8.2.-) | protein | 278 | 45% helix, 13% strand | B7ZWN4 |
| J | Sulfotransferase (EC 2.8.2.-) | protein | 274 | 47% helix, 14% strand | B7ZWN4 |
| L | Sulfotransferase (EC 2.8.2.-) | protein | 283 | 44% helix, 13% strand | B7ZWN4 |
Ligands and binding sites
- A3P · Adenosine-3'-5'-diphosphate · ligand · 12 copies · chains C, A, B, D, E, F, G, H, I, J, K, L
- CA · Calcium ion · metal · 20 copies · chains C, A, B, D, F, E, G, I, H, J, K, L
- GOL · Glycerol · additive · 2 copies · chains F, J
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
20 pockets found on a 1 Å grid, 20 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1088 | 0.87 | 0.88 | 130 | CA |
| 2 | 1019 | 0.84 | 0.85 | 81 | empty |
| 3 | 1061 | 0.83 | 0.84 | 85 | empty |
| 4 | 680 | 0.83 | 0.87 | 77 | empty |
| 5 | 375 | 0.81 | 0.90 | 61 | CA |
Interfaces
18 interfaces between chains.
- A–B · 1048 Ų buried · 17 hydrogen bonds · protein-protein
- G–I · 938 Ų buried · 20 hydrogen bonds · protein-protein
- J–K · 929 Ų buried · 15 hydrogen bonds · protein-protein
- D–E · 912 Ų buried · 18 hydrogen bonds · protein-protein
- A–I · 568 Ų buried · 3 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 1 covalent (covalent ligand).
Compared structures
- 5X2B · Crystal structure of mouse sulfotransferase SULT7A1 complexed with PAP · the same entry in another collection · chain C against C, 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 B7ZWN4
- Elsewhere: RCSB PDB 5X2B · PDBe 5X2B · UniProt B7ZWN4
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