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The crystal structure of cyclohexadienyl dehydratase precursor from pseudomonas aeruginosa PA01
Analyse The crystal structure of cyclohexadienyl dehydratase precursor from pseudomonas… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3KBR
- Type
- protein
- Length
- 231 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Cyclohexadienyl dehydratase
- EC
- 4.2.1.51, 4.2.1.91
- UniProt
- Q01269
- Ligands
- NI, CL
- Pockets
- 2 · best druggability 0.63
Structure
x-ray diffraction · 1 distinct chain · 40% helix, 23% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Cyclohexadienyl dehydratase (EC 4.2.1.51, 4.2.1.91) | protein | 231 | 40% helix, 23% strand | Q01269 |
Ligands and binding sites
- NI · Nickel (II) ion · metal · chains A
- CL · Chloride ion · ion · chains A
- GOL · Glycerol · additive · 5 copies · chains A
- FMT · Formic acid · additive · 2 copies · chains A
- EPE · 4-(2-hydroxyethyl)-1-piperazine ethanesulfonic acid · 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 | 319 | 0.63 | 0.80 | 51 | GOL, EPE |
| 2 | 51 | 0.25 | 0.73 | 15 | empty |
Modifications
Observed in the structure: 6 modified, 1 disulfide (engineered, disulfide).
Compared structures
- 3KBR · The crystal structure of cyclohexadienyl dehydratase precursor from Pseudomonas… · the same entry in another collection · chain A against A, TM-score 1.00
- Q01269 · AlphaFold monomer V2.0 prediction for cyclohexadienyl dehydratase (Q01269) · a predicted model of the same protein · chain A against A, TM-score 0.93
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 Q01269
- Elsewhere: RCSB PDB 3KBR · PDBe 3KBR · UniProt Q01269
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