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Crystal structure of a putative fumarylacetoacetate ISOMERASE/HYDROLASE from oleispira antarctica
Analyse Crystal structure of a putative fumarylacetoacetate ISOMERASE/HYDROLASE from… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3V77
- Type
- protein
- Length
- 1,344 residues
- Chains
- 6
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Putative fumarylacetoacetate ISOMERASE/HYDROLASE
- UniProt
- D2YW46
- Ligands
- ZN
- Pockets
- 17 · best druggability 0.81
Structure
x-ray diffraction · 1 distinct chain · 22% helix, 38% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D, E, F | Putative fumarylacetoacetate ISOMERASE/HYDROLASE | protein | 224 | 22% helix, 38% strand | D2YW46 |
Ligands and binding sites
- ZN · Zinc ion · metal · 7 copies · chains A, D, B, C, E, F
- TAR · D(-)-tartaric acid · additive · 9 copies · chains A, B, D, C, E, F
- ACT · Acetate ion · additive · 6 copies · chains A, B, C, D, E, F
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
17 pockets found on a 1 Å grid, 9 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1008 | 0.81 | 0.82 | 99 | TAR, ZN, ACT |
| 2 | 1014 | 0.75 | 0.78 | 89 | empty |
| 3 | 312 | 0.72 | 0.85 | 47 | TAR, ACT, ZN |
| 4 | 67 | 0.71 | 0.97 | 21 | TAR, ACT |
| 5 | 51 | 0.67 | 0.96 | 18 | TAR, ACT |
Interfaces
10 interfaces between chains.
- C–F · 1299 Ų buried · 23 hydrogen bonds · protein-protein
- A–D · 1291 Ų buried · 21 hydrogen bonds · protein-protein
- A–E · 480 Ų buried · 3 hydrogen bonds · protein-protein
- A–B · 318 Ų buried · 2 hydrogen bonds · protein-protein
- B–E · 259 Ų buried · 4 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 18 modified (engineered).
Compared structures
- 3V77 · Crystal structure of a putative fumarylacetoacetate isomerase/hydrolase from Oleispira… · 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 D2YW46
- Elsewhere: RCSB PDB 3V77 · PDBe 3V77 · UniProt D2YW46
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