MolNFT v1 · #142310 · protein
Crystal structure of human protein N-terminal asparagine amidohydrolase (NTAN1)
6A0E: “Crystal structure of human protein N-terminal asparagine amidohydrolase (NTAN1)”. X-ray diffraction, 1 ligand (PO4), 6 pockets (best druggability 0.81). MolNFT v1 #142310 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 6A0E
- Type
- protein
- Length
- 609 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Protein N-terminal asparagine amidohydrolase
- EC
- 3.5.1.-
- UniProt
- Q96AB6
- Ligands
- PO4
- Pockets
- 6 · best druggability 0.81
Structure
x-ray diffraction · 2 distinct chains · 29% helix, 27% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Protein N-terminal asparagine amidohydrolase (EC 3.5.1.-) | protein | 305 | 29% helix, 27% strand | Q96AB6 |
| B | Protein N-terminal asparagine amidohydrolase (EC 3.5.1.-) | protein | 304 | 30% helix, 26% strand | Q96AB6 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
6 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1042 | 0.81 | 0.82 | 98 | empty |
| 2 | 304 | 0.73 | 0.86 | 30 | empty |
| 3 | 456 | 0.73 | 0.83 | 50 | empty |
| 4 | 108 | 0.48 | 0.80 | 17 | GOL |
| 5 | 75 | 0.38 | 0.78 | 14 | empty |
Interfaces
1 interface between chains.
- A–B · 1108 Ų buried · 17 hydrogen bonds · protein-protein
Compared structures
- 6A0E · Crystal structure of human protein N-terminal asparagine amidohydrolase (NTAN1) · the same entry in another collection · chain A against A, TM-score 1.00
- Q96AB6 · AlphaFold monomer V2.0 prediction for protein N-terminal asparagine amidohydrolase… · a predicted model of the same protein · 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 Q96AB6
- Elsewhere: RCSB PDB 6A0E · PDBe 6A0E · UniProt Q96AB6
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