Research workbench
Crystal structure of human protein N-terminal asparagine amidohydrolase (NTAN1) C75S mutant
Analyse Crystal structure of human protein N-terminal asparagine amidohydrolase (NTAN1)… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6A0I
- 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
- 7 · best druggability 0.80
Structure
x-ray diffraction · 2 distinct chains · 28% helix, 27% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Protein N-terminal asparagine amidohydrolase (EC 3.5.1.-) | protein | 305 | 28% helix, 27% strand | Q96AB6 |
| B | Protein N-terminal asparagine amidohydrolase (EC 3.5.1.-) | protein | 304 | 28% helix, 27% strand | Q96AB6 |
Ligands and binding sites
- PO4 · Phosphate ion · ion · 3 copies · chains A, B
- GOL · Glycerol · additive · 22 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
7 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1069 | 0.80 | 0.82 | 96 | GOL |
| 2 | 436 | 0.74 | 0.84 | 46 | GOL |
| 3 | 364 | 0.73 | 0.84 | 40 | GOL |
| 4 | 114 | 0.51 | 0.82 | 16 | GOL |
| 5 | 82 | 0.41 | 0.79 | 18 | empty |
Interfaces
1 interface between chains.
- A–B · 1174 Ų buried · 18 hydrogen bonds · protein-protein
Compared structures
- 6A0I · Crystal structure of human protein N-terminal asparagine amidohydrolase (NTAN1) C75S… · 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 6A0I · PDBe 6A0I · UniProt Q96AB6
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