Research workbench
NMR structure of P. aeruginosa protein PA1324: northeast structural genomics consortium target PAP1
Analyse NMR structure of P. aeruginosa protein PA1324: northeast structural genomics… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1XPN
- Type
- protein
- Length
- 170 residues
- Chains
- 1
- Method
- solution nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Hypothetical protein PA1324
- UniProt
- Q9I420
- Pockets
- 2 · best druggability 0.49
Structure
solution nmr · 1 distinct chain · 11% helix, 36% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Hypothetical protein PA1324 | protein | 170 | 11% helix, 36% strand | Q9I420 |
Pockets
2 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 171 | 0.49 | 0.77 | 25 | empty |
| 2 | 82 | 0.37 | 0.77 | 16 | empty |
Compared structures
- 1XPN · NMR structure of P. aeruginosa protein PA1324: Northeast Structural Genomics Consortium… · 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 Q9I420
- Elsewhere: RCSB PDB 1XPN · PDBe 1XPN · UniProt Q9I420
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