Research workbench
Crystal structures of dmsp lyases rddddp and rndddqii
Analyse Crystal structures of dmsp lyases rddddp and rndddqii in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4B29
- Type
- protein
- Length
- 195 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Dimethylsulfoniopropionate lyase
- UniProt
- A3SNG1
- Ligands
- ZN, NI, BR, PO4
- Pockets
- 1 · best druggability 0.71
Structure
x-ray diffraction · 1 distinct chain · 28% helix, 32% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Dimethylsulfoniopropionate lyase | protein | 195 | 28% helix, 32% strand | A3SNG1 |
Ligands and binding sites
- ZN · Zinc ion · metal · chains A
- NI · Nickel (II) ion · metal · chains A
- BR · Bromide ion · ion · 5 copies · chains A
- PO4 · Phosphate ion · ion · 4 copies · chains A
- EDO · 1,2-ethanediol · additive · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 61 | 0.71 | 0.97 | 21 | PO4, EDO |
Compared structures
- 4B29 · Crystal structures of DMSP lyases RdDddP and RnDddQII · 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 A3SNG1
- Elsewhere: RCSB PDB 4B29 · PDBe 4B29 · UniProt A3SNG1
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