Research workbench
Penicillin acylase complexed with thiopheneacetic acid
Analyse Penicillin acylase complexed with thiopheneacetic acid in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1AJQ
- Type
- protein
- Length
- 763 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Penicillin amidohydrolase
- EC
- 3.5.1.11
- UniProt
- P06875
- Ligands
- SPA, CA
- Pockets
- 9 · best druggability 0.61
Structure
x-ray diffraction · 2 distinct chains · 35% helix, 22% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Penicillin amidohydrolase (EC 3.5.1.11) | protein | 206 | 63% helix, 6% strand | P06875 |
| B | Penicillin amidohydrolase (EC 3.5.1.11) | protein | 557 | 25% helix, 27% strand | P06875 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
9 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 385 | 0.61 | 0.77 | 42 | SPA |
| 2 | 194 | 0.47 | 0.75 | 29 | empty |
| 3 | 112 | 0.43 | 0.77 | 19 | empty |
| 4 | 121 | 0.41 | 0.75 | 20 | empty |
| 5 | 76 | 0.41 | 0.79 | 17 | empty |
Interfaces
1 interface between chains.
- A–B · 7184 Ų buried · 122 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 P06875
- Elsewhere: RCSB PDB 1AJQ · PDBe 1AJQ · UniProt P06875
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