MolNFT v2 · #157427 · protein
Structure of the 2-Aminoisobutyric acid Monooxygenase Hydroxylase
6M2I: “Structure of the 2-Aminoisobutyric acid Monooxygenase Hydroxylase”. X-ray diffraction at 2.45, 3 ligands (FE, ZN, SO4). MolNFT v2 #157427 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 6M2I
- Type
- protein
- Length
- 708 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 2.45
- Source
- Rhodococcus wratislaviensis
- UniProt
- A0A402C2V4, A0A402C2Q3
- Ligands
- FE, ZN, SO4
Structure
x-ray diffraction · resolution 2.45 · 2 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 354 | — | A0A402C2V4 |
| B | — | protein | 354 | — | A0A402C2Q3 |
Ligands and binding sites
- FE · Fe (III) ion · metal · 2 copies · chains B
- ZN · Zinc ion · metal · chains A
- SO4 · Sulfate ion · ion · 5 copies · chains A, B
- EDO · 1,2-ethanediol · additive · 17 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 6M2I · Structure of the 2-aminoisobutyric acid monooxygenase hydroxylase · the same entry in another collection · chain A against A, 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 A0A402C2V4
- Every structure of UniProt A0A402C2Q3
- Elsewhere: RCSB PDB 6M2I · PDBe 6M2I · UniProt A0A402C2V4 · UniProt A0A402C2Q3
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