Research workbench
Crystal structure of mouse fumarylacetoacetate hydrolase refined at 1.55 ångström resolution
Analyse Crystal structure of mouse fumarylacetoacetate hydrolase refined at 1.55… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1QQJ
- Type
- protein
- Length
- 832 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Fumarylacetoacetate hydrolase
- EC
- 3.7.1.2
- UniProt
- P35505
- Ligands
- CA
- Pockets
- 7 · best druggability 0.70
Structure
x-ray diffraction · 1 distinct chain · 24% helix, 28% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Fumarylacetoacetate hydrolase (EC 3.7.1.2) | protein | 416 | 24% helix, 28% strand | P35505 |
Ligands and binding sites
- CA · Calcium ion · metal · 2 copies · chains A, B
- ACT · Acetate ion · additive · 2 copies · chains A, B
- CAC · Cacodylate ion · additive · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
7 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 194 | 0.70 | 0.87 | 42 | ACT, CAC |
| 2 | 289 | 0.68 | 0.83 | 51 | CA, ACT, CAC |
| 3 | 173 | 0.42 | 0.74 | 37 | empty |
| 4 | 76 | 0.39 | 0.78 | 17 | empty |
| 5 | 55 | 0.37 | 0.80 | 16 | empty |
Interfaces
1 interface between chains.
- A–B · 2815 Ų buried · 45 hydrogen bonds · protein-protein
Compared structures
- 1QQJ · Crystal structure of mouse fumarylacetoacetate hydrolase refined at 1.55 ångström… · the same entry in another collection · chain A against A, TM-score 1.00
- P35505 · AlphaFold monomer V2.0 prediction for fumarylacetoacetase (P35505) · a predicted model of the same protein · chain B 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 P35505
- Elsewhere: RCSB PDB 1QQJ · PDBe 1QQJ · UniProt P35505
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