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The crystal structure of ecaah in complex with allantoate
Analyse The crystal structure of ecaah in complex with allantoate in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4PXD
- Type
- protein
- Length
- 822 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Allantoate amidohydrolase
- EC
- 3.5.3.-
- UniProt
- P77425
- Ligands
- 1AL, MN
- Pockets
- 3 · best druggability 0.67
Structure
x-ray diffraction · 1 distinct chain · 38% helix, 26% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Allantoate amidohydrolase (EC 3.5.3.-) | protein | 411 | 38% helix, 26% strand | P77425 |
Ligands and binding sites
- 1AL · Allantoate ion · ligand · 2 copies · chains A, B
- MN · Manganese (II) ion · metal · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 617 | 0.67 | 0.77 | 68 | empty |
| 2 | 125 | 0.54 | 0.82 | 27 | empty |
| 3 | 137 | 0.53 | 0.81 | 28 | empty |
Interfaces
1 interface between chains.
- A–B · 2577 Ų buried · 33 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 P77425
- Elsewhere: RCSB PDB 4PXD · PDBe 4PXD · UniProt P77425
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