Research workbench
Stenotrophomonas maltophilia DPP7 in complex with val-tyr
Analyse Stenotrophomonas maltophilia DPP7 in complex with val-tyr in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7DKB
- Type
- protein
- Length
- 1,398 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Dipeptidyl-peptidase
- EC
- 3.4.14.-
- UniProt
- B4SLK2
- Pockets
- 16 · best druggability 0.75
Structure
x-ray diffraction · 1 distinct chain · 50% helix, 16% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Dipeptidyl-peptidase (EC 3.4.14.-) | protein | 699 | 50% helix, 16% strand | B4SLK2 |
Pockets
16 pockets found on a 1 Å grid, 8 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 593 | 0.75 | 0.82 | 72 | empty |
| 2 | 938 | 0.74 | 0.78 | 87 | empty |
| 3 | 661 | 0.71 | 0.78 | 77 | empty |
| 4 | 803 | 0.71 | 0.76 | 54 | empty |
| 5 | 364 | 0.69 | 0.82 | 62 | empty |
Interfaces
1 interface between chains.
- A–B · 614 Ų buried · 19 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 4 disulfide (disulfide).
Compared structures
- 7DKB · Stenotrophomonas maltophilia DPP7 in complex with Val-Tyr · 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 B4SLK2
- Elsewhere: RCSB PDB 7DKB · PDBe 7DKB · UniProt B4SLK2
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