MolNFT v1 · #92148 · protein
Human aminopeptidase N (CD13)
4FYQ: “Human aminopeptidase N (CD13)”. X-ray diffraction, 4 ligands (NAG, BMA, ZN), 7 pockets (best druggability 0.72). MolNFT v1 #92148 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 4FYQ
- Type
- protein
- Length
- 892 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Aminopeptidase N
- EC
- 3.4.11.2
- UniProt
- P15144
- Ligands
- NAG, BMA, ZN, SO4
- Pockets
- 7 · best druggability 0.72
Structure
x-ray diffraction · 1 distinct chain · 47% helix, 20% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Aminopeptidase N (EC 3.4.11.2) | protein | 892 | 47% helix, 20% strand | P15144 |
Ligands and binding sites
- NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 10 copies · chains A
- BMA · beta-D-mannopyranose · sugar
- ZN · Zinc ion · metal · chains A
- SO4 · Sulfate ion · ion · 11 copies · chains A
- ACY · Acetic acid · additive · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
7 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 281 | 0.72 | 0.86 | 41 | empty |
| 2 | 312 | 0.65 | 0.81 | 40 | SO4 |
| 3 | 159 | 0.57 | 0.82 | 27 | empty |
| 4 | 108 | 0.56 | 0.85 | 22 | empty |
| 5 | 136 | 0.55 | 0.82 | 27 | ACY |
Modifications
Observed in the structure: 8 glycan, 2 disulfide (N-glycosylation, disulfide).
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 P15144
- Elsewhere: RCSB PDB 4FYQ · PDBe 4FYQ · UniProt P15144
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