Research workbench
Crystal structure of human SPLUNC1 lacking the secretion signal sequence
Analyse Crystal structure of human SPLUNC1 lacking the secretion signal sequence in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4KGH
- Type
- protein
- Length
- 390 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Bpi fold-containing family a member 1
- UniProt
- Q9NP55
- Ligands
- NA, NO3, NH4
- Pockets
- 1 · best druggability 0.36
Structure
x-ray diffraction · 2 distinct chains · 38% helix, 31% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| B | Bpi fold-containing family a member 1 | protein | 197 | 40% helix, 31% strand | Q9NP55 |
| A | Bpi fold-containing family a member 1 | protein | 193 | 36% helix, 30% strand | Q9NP55 |
Ligands and binding sites
- NA · Sodium ion · metal · chains B
- NO3 · Nitrate ion · ion · chains B, A
- NH4 · Ammonium ion · ion · chains B
- GOL · Glycerol · additive · chains B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 91 | 0.36 | 0.74 | 15 | empty |
Interfaces
1 interface between chains.
- B–A · 780 Ų buried · 5 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 2 disulfide (disulfide).
Compared structures
- 4KGH · Crystal Structure of human splunc1 lacking the secretion signal sequence · the same entry in another collection · chain B against B, TM-score 1.00
- Q9NP55 · AlphaFold monomer V2.0 prediction for bpi fold-containing family a member 1 (Q9NP55) · a predicted model of the same protein · chain A against A, TM-score 0.87
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 Q9NP55
- Elsewhere: RCSB PDB 4KGH · PDBe 4KGH · UniProt Q9NP55
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