MolNFT v1 · #126099 · protein
Ethylene forming enzyme from pseudomonas syringae pv. phaseolicola - I222 crystal form
5LSQ: “Ethylene forming enzyme from pseudomonas syringae pv. phaseolicola - I222 crystal form”. X-ray diffraction, 2 ligands (MN, CL), 2 pockets (best druggability 0.76). MolNFT v1 #126099 on GenesisL1: 3D structure, binding sites and…
- PDB
- 5LSQ
- Type
- protein
- Length
- 342 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Ethylene forming enzyme
- UniProt
- P32021
- Ligands
- MN, CL
- Pockets
- 2 · best druggability 0.76
Structure
x-ray diffraction · 1 distinct chain · 31% helix, 19% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Ethylene forming enzyme | protein | 342 | 31% helix, 19% strand | P32021 |
Ligands and binding sites
- MN · Manganese (II) ion · metal · chains A
- CL · Chloride ion · ion · chains A
- GOL · Glycerol · additive · 2 copies · chains A
- B3P · 2-[3-(2-hydroxy-1,1-dihydroxymethyl-ethylamino)-propylamino]-2-hydroxymethyl-propane-1,3-diol · additive · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 436 | 0.76 | 0.85 | 65 | CL, B3P |
| 2 | 136 | 0.42 | 0.75 | 20 | empty |
Compared structures
- 5LSQ · Ethylene Forming Enzyme from Pseudomonas syringae pv. phaseolicola - I222 crystal form · the same entry in another collection · chain A against A, TM-score 1.00
- P32021 · AlphaFold monomer V2.0 prediction for 2-oxoglutarate-dependent ETHYLENE/SUCCINATE-forming… · a predicted model of the same protein · chain A against A, TM-score 0.98
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 P32021
- Elsewhere: RCSB PDB 5LSQ · PDBe 5LSQ · UniProt P32021
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