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Crystal structure of homoprotocatechuate 2,3-dioxygenase from arthrobacter globiformis (native, low temperature)
Analyse Crystal structure of homoprotocatechuate 2,3-dioxygenase from arthrobacter… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1F1U
- Type
- protein
- Length
- 643 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Homoprotocatechuate 2,3-dioxygenase
- EC
- 1.13.11.15
- UniProt
- Q44048
- Ligands
- MN
- Pockets
- 5 · best druggability 0.87
Structure
x-ray diffraction · 2 distinct chains · 19% helix, 37% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Homoprotocatechuate 2,3-dioxygenase (EC 1.13.11.15) | protein | 322 | 19% helix, 36% strand | Q44048 |
| B | Homoprotocatechuate 2,3-dioxygenase (EC 1.13.11.15) | protein | 321 | 19% helix, 37% strand | Q44048 |
Ligands and binding sites
- MN · Manganese (II) ion · metal · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
5 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 431 | 0.87 | 0.95 | 40 | empty |
| 2 | 174 | 0.66 | 0.86 | 36 | MN |
| 3 | 203 | 0.64 | 0.84 | 35 | empty |
| 4 | 262 | 0.58 | 0.79 | 28 | empty |
| 5 | 63 | 0.32 | 0.76 | 18 | empty |
Interfaces
1 interface between chains.
- A–B · 1670 Ų buried · 38 hydrogen bonds · protein-protein
Compared structures
- 1F1U · Crystal structure of homoprotocatechuate 2,3-dioxygenase from arthrobacter globiformis… · 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 Q44048
- Elsewhere: RCSB PDB 1F1U · PDBe 1F1U · UniProt Q44048
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