MolNFT v1 · #58492 · protein
Crystal structure of indole-3-acetic acid methyltransferase
3B5I · S-adenosyl-L-METHIONINE:SALICYLIC acid carboxyl…: “Crystal structure of indole-3-acetic acid methyltransferase”. X-ray diffraction, 2 ligands (SAH, MG), 4 pockets (best druggability 0.69). MolNFT v1 #58492 on GenesisL1: 3D…
- PDB
- 3B5I
- Type
- protein
- Length
- 684 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- S-adenosyl-L-METHIONINE:SALICYLIC acid carboxyl methyltransferase-like protein
- UniProt
- Q9FLN8
- Ligands
- SAH, MG
- Pockets
- 4 · best druggability 0.69
Structure
x-ray diffraction · 2 distinct chains · 40% helix, 18% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | S-adenosyl-L-METHIONINE:SALICYLIC acid carboxyl methyltransferase-like protein | protein | 344 | 41% helix, 18% strand | Q9FLN8 |
| B | S-adenosyl-L-METHIONINE:SALICYLIC acid carboxyl methyltransferase-like protein | protein | 340 | 40% helix, 18% strand | Q9FLN8 |
Ligands and binding sites
- SAH · S-adenosyl-L-homocysteine · ligand · 2 copies · chains A, B
- MG · Magnesium ion · metal · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
4 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 255 | 0.69 | 0.84 | 34 | empty |
| 2 | 679 | 0.68 | 0.76 | 59 | SAH |
| 3 | 595 | 0.66 | 0.76 | 61 | SAH |
| 4 | 91 | 0.33 | 0.74 | 19 | empty |
Interfaces
1 interface between chains.
- A–B · 1047 Ų buried · 17 hydrogen bonds · protein-protein
Compared structures
- 3B5I · Crystal structure of Indole-3-acetic Acid Methyltransferase · the same entry in another collection · chain A against A, TM-score 1.00
- Q9FLN8 · AlphaFold monomer V2.0 prediction for indole-3-acetate O-methyltransferase 1 (Q9FLN8) · a predicted model of the same protein · chain B against A, TM-score 0.99
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 Q9FLN8
- Elsewhere: RCSB PDB 3B5I · PDBe 3B5I · UniProt Q9FLN8
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