Research workbench
Crystal structure of putative 4-amino-4-deoxychorismate lyase. (YP_094631.1) from legionella pneumophila subsp. pneumophila str. philadelphia 1 at 1.78 a resolution
Analyse Crystal structure of putative 4-amino-4-deoxychorismate lyase. (YP_094631.1)… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3LUL
- Type
- protein
- Length
- 537 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- 4-amino-4-deoxychorismate lyase
- UniProt
- Q5ZXY5
- Ligands
- PO4
- Pockets
- 7 · best druggability 0.79
Structure
x-ray diffraction · 2 distinct chains · 30% helix, 31% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | 4-amino-4-deoxychorismate lyase | protein | 268 | 31% helix, 31% strand | Q5ZXY5 |
| B | 4-amino-4-deoxychorismate lyase | protein | 269 | 30% helix, 30% strand | Q5ZXY5 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
7 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 121 | 0.79 | 0.98 | 33 | empty |
| 2 | 506 | 0.77 | 0.85 | 47 | empty |
| 3 | 509 | 0.76 | 0.84 | 46 | EDO |
| 4 | 95 | 0.49 | 0.82 | 20 | empty |
| 5 | 115 | 0.47 | 0.80 | 27 | empty |
Interfaces
1 interface between chains.
- A–B · 2080 Ų buried · 29 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 10 modified (engineered, cofactor).
Compared structures
- 3LUL · Crystal structure of Putative 4-amino-4-deoxychorismate lyase. (YP_094631.1) from… · 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 Q5ZXY5
- Elsewhere: RCSB PDB 3LUL · PDBe 3LUL · UniProt Q5ZXY5
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