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The crystal structure of an amidohydrolase from mycoplasma synoviae
Analyse The crystal structure of an amidohydrolase from mycoplasma synoviae in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3MSR
- Type
- protein
- Length
- 353 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Amidohydrolases
- UniProt
- Q4A724
- Ligands
- PO4
- Pockets
- 1 · best druggability 0.65
Structure
x-ray diffraction · 1 distinct chain · 49% helix, 15% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Amidohydrolases | protein | 353 | 49% helix, 15% strand | Q4A724 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 175 | 0.65 | 0.85 | 28 | PO4 |
Modifications
Observed in the structure: 6 modified (engineered).
Compared structures
- 3MSR · The crystal structure of an amidohydrolase from Mycoplasma synoviae · the same entry in another collection · chain A against A, TM-score 1.00
- Q4A724 · AlphaFold monomer V2.0 prediction for phospho-furanose lactonase (Q4A724) · a predicted model of the same protein · 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 Q4A724
- Elsewhere: RCSB PDB 3MSR · PDBe 3MSR · UniProt Q4A724
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