Research workbench
High resolution (2.2 a) crystal structure of wbdd.
Analyse High resolution (2.2 a) crystal structure of wbdd. in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4AZS
- Type
- protein
- Length
- 442 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Methyltransferase wbdd
- UniProt
- Q47592
- Ligands
- AMP, SAM, SO4, CL
- Pockets
- 3 · best druggability 0.65
Structure
x-ray diffraction · 1 distinct chain · 41% helix, 21% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Methyltransferase wbdd | protein | 442 | 41% helix, 21% strand | Q47592 |
Ligands and binding sites
- AMP · Adenosine monophosphate · ligand · chains A
- SAM · S-adenosylmethionine · ligand · chains A
- SO4 · Sulfate ion · ion · 11 copies · chains A
- CL · Chloride ion · ion · 2 copies · 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, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 236 | 0.65 | 0.83 | 36 | SAM |
| 2 | 310 | 0.62 | 0.79 | 38 | AMP |
| 3 | 68 | 0.39 | 0.79 | 20 | SO4 |
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 Q47592
- Elsewhere: RCSB PDB 4AZS · PDBe 4AZS · UniProt Q47592
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