Research workbench
Pandda analysis group deposition of ground-state model of porphyromonas gingivalis DPP11
Analyse Pandda analysis group deposition of ground-state model of porphyromonas… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5SDS
- Type
- protein
- Length
- 1,392 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- ASP/GLU-specific dipeptidyl-peptidase
- EC
- 3.4.14.-
- UniProt
- B2RID1
- Ligands
- CL
- Pockets
- 11 · best druggability 0.70
Structure
x-ray diffraction · 2 distinct chains · 51% helix, 16% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | ASP/GLU-specific dipeptidyl-peptidase (EC 3.4.14.-) | protein | 697 | 51% helix, 16% strand | B2RID1 |
| B | ASP/GLU-specific dipeptidyl-peptidase (EC 3.4.14.-) | protein | 695 | 51% helix, 16% strand | B2RID1 |
Ligands and binding sites
- CL · Chloride ion · ion · 3 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
11 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 770 | 0.70 | 0.77 | 79 | empty |
| 2 | 770 | 0.70 | 0.77 | 77 | empty |
| 3 | 273 | 0.50 | 0.73 | 39 | empty |
| 4 | 85 | 0.38 | 0.76 | 19 | empty |
| 5 | 106 | 0.36 | 0.74 | 14 | empty |
Interfaces
1 interface between chains.
- A–B · 717 Ų buried · 25 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 2 disulfide (disulfide).
Compared structures
- 5SDS · PanDDA analysis group deposition of ground-state model of Porphyromonas gingivalis DPP11 · the same entry in another collection · chain A against A, TM-score 1.00
- B2RID1 · AlphaFold monomer V2.0 prediction for ASP/GLU-specific dipeptidyl- peptidase (B2RID1) · a predicted model of the same protein · chain B against A, TM-score 0.91
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 B2RID1
- Elsewhere: RCSB PDB 5SDS · PDBe 5SDS · UniProt B2RID1
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