Research workbench
Crystal structure of R138Q mutant of recombinant sulfite oxidase at resting state
Analyse Crystal structure of R138Q mutant of recombinant sulfite oxidase at resting… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2A9B
- Type
- protein
- Length
- 372 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Sulfite oxidase
- EC
- 1.8.3.1
- UniProt
- P07850
- Ligands
- MTE, MO, CL
- Pockets
- 3 · best druggability 0.78
Structure
x-ray diffraction · 1 distinct chain · 12% helix, 36% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Sulfite oxidase (EC 1.8.3.1) | protein | 372 | 12% helix, 36% strand | P07850 |
Ligands and binding sites
- MTE · Phosphonic acidmono-(2-amino-5,6-dimercapto-4-oxo-3,7,8A,9,10,10A-hexahydro-4H-8-oxa-1,3,9,10-tetraaza-anthracen-7-ylmethyl)ester · ligand · chains A
- MO · Molybdenum atom · metal · chains A
- CL · Chloride ion · ion · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 93 | 0.78 | 0.98 | 25 | MTE, MO |
| 2 | 135 | 0.49 | 0.79 | 23 | empty |
| 3 | 60 | 0.33 | 0.77 | 21 | CL |
Compared structures
- 2A9B · Crystal structure of R138Q mutant of recombinant sulfite oxidase at resting state · the same entry in another collection · chain A against A, TM-score 1.00
- P07850 · AlphaFold monomer V2.0 prediction for sulfite oxidase (P07850) · a predicted model of the same protein · chain A 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 P07850
- Elsewhere: RCSB PDB 2A9B · PDBe 2A9B · UniProt P07850
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