MolNFT v1 · #142313 · protein
Crystal structure of human protein N-terminal asparagine amidohydrolase (NTAN1) C75S mutant with asn-leu-ala-ala-arg peptide
6A0H: “Crystal structure of human protein N-terminal asparagine amidohydrolase (NTAN1) C75S mutant with…”. X-ray diffraction, 1 ligand (PO4), 5 pockets (best druggability 0.80). MolNFT v1 #142313 on GenesisL1: 3D structure, binding sites…
- PDB
- 6A0H
- Type
- protein
- Length
- 611 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Protein N-terminal asparagine amidohydrolase; 5-mer peptide asn-leu-ala-ala-arg
- EC
- 3.5.1.-
- UniProt
- Q96AB6
- Ligands
- PO4
- Pockets
- 5 · best druggability 0.80
Structure
x-ray diffraction · 4 distinct chains · 29% helix, 28% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Protein N-terminal asparagine amidohydrolase (EC 3.5.1.-) | protein | 302 | 29% helix, 28% strand | Q96AB6 |
| B | Protein N-terminal asparagine amidohydrolase (EC 3.5.1.-) | protein | 302 | 29% helix, 27% strand | Q96AB6 |
| C | 5-mer peptide asn-leu-ala-ala-arg | protein | 4 | 0% helix, 25% strand | — |
| D | 5-mer peptide asn-leu-ala-ala-arg | protein | 3 | 0% helix, 33% strand | — |
Ligands and binding sites
- PO4 · Phosphate ion · ion · 6 copies · chains A, B
- GOL · Glycerol · additive · 5 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
5 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1145 | 0.80 | 0.81 | 98 | empty |
| 2 | 180 | 0.70 | 0.88 | 25 | empty |
| 3 | 108 | 0.52 | 0.82 | 19 | empty |
| 4 | 130 | 0.42 | 0.76 | 20 | empty |
| 5 | 103 | 0.36 | 0.74 | 22 | empty |
Interfaces
3 interfaces between chains.
- A–B · 954 Ų buried · 11 hydrogen bonds · protein-protein
- A–C · 421 Ų buried · 10 hydrogen bonds · protein-protein
- B–D · 377 Ų buried · 11 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 1 covalent (additive adduct).
Compared structures
- 6A0H · 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 B against A, TM-score 0.99
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 6A0H · PDBe 6A0H · UniProt Q96AB6
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