Research workbench
Crystal structure of E. COLI aconitase B.
Analyse Crystal structure of E. COLI aconitase B. in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1L5J
- Type
- protein
- Length
- 1,724 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Aconitate hydratase 2
- EC
- 4.2.1.3
- UniProt
- P36683
- Ligands
- TRA, F3S
- Pockets
- 20 · best druggability 0.77
Structure
x-ray diffraction · 1 distinct chain · 42% helix, 16% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Aconitate hydratase 2 (EC 4.2.1.3) | protein | 862 | 42% helix, 16% strand | P36683 |
Ligands and binding sites
- TRA · Aconitate ion · ligand · 2 copies · chains A, B
- F3S · FE3-S4 cluster · ligand · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
20 pockets found on a 1 Å grid, 11 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 620 | 0.77 | 0.83 | 65 | empty |
| 2 | 699 | 0.77 | 0.82 | 67 | empty |
| 3 | 777 | 0.75 | 0.80 | 101 | empty |
| 4 | 78 | 0.75 | 0.98 | 25 | TRA, F3S |
| 5 | 663 | 0.74 | 0.80 | 77 | empty |
Interfaces
1 interface between chains.
- A–B · 985 Ų buried · 14 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 P36683
- Elsewhere: RCSB PDB 1L5J · PDBe 1L5J · UniProt P36683
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