Research workbench
Crystal structure of PAM12A
Analyse Crystal structure of PAM12A in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5AC3
- Type
- protein
- Length
- 490 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Peptide amidase
- EC
- 3.5.1.4
- UniProt
- Q8RJN5
- Ligands
- CD
- Pockets
- 4 · best druggability 0.67
Structure
x-ray diffraction · 1 distinct chain · 39% helix, 15% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Peptide amidase (EC 3.5.1.4) | protein | 490 | 39% helix, 15% strand | Q8RJN5 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
4 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 369 | 0.67 | 0.80 | 30 | ACY |
| 2 | 121 | 0.57 | 0.84 | 23 | empty |
| 3 | 101 | 0.43 | 0.78 | 17 | empty |
| 4 | 63 | 0.31 | 0.75 | 18 | empty |
Modifications
Observed in the structure: 1 disulfide (disulfide).
Compared structures
- 5AC3 · Crystal structure of PAM12A · 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 Q8RJN5
- Elsewhere: RCSB PDB 5AC3 · PDBe 5AC3 · UniProt Q8RJN5
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