Research workbench
Crystal structure of a merb-triimethyllead complex.
Analyse Crystal structure of a merb-triimethyllead complex. in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5U88
- Type
- protein
- Length
- 416 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Alkylmercury lyase
- EC
- 4.99.1.2
- UniProt
- P77072
- Ligands
- ZN9
- Pockets
- 5 · best druggability 0.81
Structure
x-ray diffraction · 1 distinct chain · 42% helix, 22% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Alkylmercury lyase (EC 4.99.1.2) | protein | 208 | 42% helix, 22% strand | P77072 |
Ligands and binding sites
- ZN9 · Trimethyllead bromide · ligand · 2 copies · chains A, B
- ACT · Acetate ion · additive · 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, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1015 | 0.81 | 0.83 | 83 | ACT |
| 2 | 233 | 0.80 | 0.93 | 35 | ZN9 |
| 3 | 204 | 0.75 | 0.90 | 34 | ZN9 |
| 4 | 115 | 0.42 | 0.77 | 15 | empty |
| 5 | 99 | 0.37 | 0.75 | 17 | empty |
Interfaces
1 interface between chains.
- A–B · 954 Ų buried · 13 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 P77072
- Elsewhere: RCSB PDB 5U88 · PDBe 5U88 · UniProt P77072
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