Research workbench
Crystal structure of N-terminal amidase with asn-glu-ala peptide
Analyse Crystal structure of N-terminal amidase with asn-glu-ala peptide in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5B62
- Type
- protein
- Length
- 429 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- NTA1P; Asn-glu-ala
- UniProt
- N1P8Q8
- Pockets
- 4 · best druggability 0.55
Structure
x-ray diffraction · 2 distinct chains · 25% helix, 26% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | NTA1P | protein | 426 | 25% helix, 26% strand | N1P8Q8 |
| B | Asn-glu-ala | protein | 3 | 0% helix, 0% strand | — |
Pockets
4 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 182 | 0.55 | 0.80 | 30 | empty |
| 2 | 142 | 0.49 | 0.79 | 23 | empty |
| 3 | 69 | 0.39 | 0.79 | 15 | empty |
| 4 | 63 | 0.31 | 0.75 | 21 | empty |
Interfaces
1 interface between chains.
- A–B · 325 Ų buried · 6 hydrogen bonds · protein-protein
Compared structures
- 5B62 · Crystal structure of N-terminal amidase with Asn-Glu-Ala peptide · 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 N1P8Q8
- Elsewhere: RCSB PDB 5B62 · PDBe 5B62 · UniProt N1P8Q8
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