Research workbench
Meta-cleavage product hydrolase from pseudomonas fluorescens IP01 (cumd) S103A mutant complexed with acetates
Analyse Meta-cleavage product hydrolase from pseudomonas fluorescens IP01 (cumd) S103A… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1IUO
- Type
- protein
- Length
- 272 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Meta-cleavage product hydrolase
- EC
- 3.7.1.9
- UniProt
- P96965
- Pockets
- 1 · best druggability 0.81
Structure
x-ray diffraction · 1 distinct chain · 43% helix, 18% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Meta-cleavage product hydrolase (EC 3.7.1.9) | protein | 272 | 43% helix, 18% strand | P96965 |
Ligands and binding sites
- ACT · Acetate ion · additive · 2 copies · chains A
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 | 275 | 0.81 | 0.92 | 45 | ACT |
Compared structures
- 1IUO · meta-Cleavage product hydrolase from Pseudomonas fluorescens IP01 (CumD) S103A mutant… · 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 P96965
- Elsewhere: RCSB PDB 1IUO · PDBe 1IUO · UniProt P96965
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