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Physiological dimer hpp precursor
Analyse Physiological dimer hpp precursor in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1IVY
- Type
- protein
- Length
- 902 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Human protective protein
- EC
- 3.4.16.5
- UniProt
- P10619
- Ligands
- NAG, NDG
- Pockets
- 12 · best druggability 0.75
Structure
x-ray diffraction · 2 distinct chains · 32% helix, 23% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Human protective protein (EC 3.4.16.5) | protein | 452 | 33% helix, 23% strand | P10619 |
| B | Human protective protein (EC 3.4.16.5) | protein | 450 | 32% helix, 22% strand | P10619 |
Ligands and binding sites
- NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 5 copies · chains A, B
- NDG · 2-acetamido-2-deoxy-alpha-D-glucopyranose · sugar
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
12 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 448 | 0.75 | 0.84 | 58 | empty |
| 2 | 566 | 0.74 | 0.82 | 60 | empty |
| 3 | 279 | 0.58 | 0.78 | 37 | empty |
| 4 | 294 | 0.56 | 0.76 | 30 | empty |
| 5 | 254 | 0.53 | 0.76 | 28 | empty |
Interfaces
1 interface between chains.
- A–B · 1679 Ų buried · 17 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 8 disulfide, 4 glycan (disulfide, N-glycosylation).
Compared structures
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 P10619
- Elsewhere: RCSB PDB 1IVY · PDBe 1IVY · UniProt P10619
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