Research workbench
Fe-succinate complex of atsk
Analyse Fe-succinate complex of atsk in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1VZ4
- Type
- protein
- Length
- 508 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Putative alkylsulfatase atsk
- UniProt
- Q9WWU5
- Ligands
- FE2
- Pockets
- 4 · best druggability 0.70
Structure
x-ray diffraction · 2 distinct chains · 21% helix, 30% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Putative alkylsulfatase atsk | protein | 249 | 22% helix, 31% strand | Q9WWU5 |
| D | Putative alkylsulfatase atsk | protein | 259 | 20% helix, 30% strand | Q9WWU5 |
Ligands and binding sites
- FE2 · Fe (II) ion · metal · 2 copies · chains A, D
- SIN · Succinic acid · additive · 2 copies · chains A, D
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 | 71 | 0.70 | 0.95 | 22 | SIN |
| 2 | 51 | 0.68 | 0.97 | 20 | SIN |
| 3 | 294 | 0.60 | 0.79 | 29 | empty |
| 4 | 193 | 0.49 | 0.76 | 27 | empty |
Interfaces
1 interface between chains.
- A–D · 885 Ų buried · 24 hydrogen bonds · protein-protein
Compared structures
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 Q9WWU5
- Elsewhere: RCSB PDB 1VZ4 · PDBe 1VZ4 · UniProt Q9WWU5
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