Research workbench
Crystal structure of the aminopeptidase N family protein Q5QTY1 from idiomarina loihiensis. northeast structural genomics consortium target ILR60.
Analyse Crystal structure of the aminopeptidase N family protein Q5QTY1 from idiomarina… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4FGM
- Type
- protein
- Length
- 587 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Aminopeptidase N family protein
- EC
- 3.4.11.2
- UniProt
- Q5QTY1
- Ligands
- MAE, ZN
- Pockets
- 5 · best druggability 0.66
Structure
x-ray diffraction · 1 distinct chain · 29% helix, 28% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Aminopeptidase N family protein (EC 3.4.11.2) | protein | 587 | 29% helix, 28% strand | Q5QTY1 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
5 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 580 | 0.66 | 0.77 | 56 | MAE |
| 2 | 86 | 0.37 | 0.76 | 19 | empty |
| 3 | 79 | 0.35 | 0.76 | 18 | empty |
| 4 | 50 | 0.28 | 0.75 | 12 | empty |
| 5 | 60 | 0.27 | 0.73 | 13 | empty |
Modifications
Observed in the structure: 9 modified (engineered).
Compared structures
- 4FGM · Crystal structure of the aminopeptidase N family protein Q5QTY1 from Idiomarina… · 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 Q5QTY1
- Elsewhere: RCSB PDB 4FGM · PDBe 4FGM · UniProt Q5QTY1
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