MolNFT v1 · #31089 · protein
Porcine dipeptidyl peptidase IV (CD26) in complex with 7-benzyl-1,3- dimethyl-8-piperazin-1-yl-3,7-dihydro-purine-2,6-dione (bdpx)
2AJ8 · Dipeptidyl peptidase 4: “Porcine dipeptidyl peptidase IV (CD26) in complex with 7-benzyl-1,3…”. X-ray diffraction, 4 ligands (SC3, NAG, BMA), 20 pockets (best druggability 0.74). MolNFT v1 #31089 on GenesisL1: 3D structure, binding…
- PDB
- 2AJ8
- Type
- protein
- Length
- 2,912 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Dipeptidyl peptidase 4
- EC
- 3.4.14.5
- UniProt
- P22411
- Ligands
- SC3, NAG, BMA, SO4
- Pockets
- 20 · best druggability 0.74
Structure
x-ray diffraction · 1 distinct chain · 18% helix, 38% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D | Dipeptidyl peptidase 4 (EC 3.4.14.5) | protein | 728 | 18% helix, 38% strand | P22411 |
Ligands and binding sites
- SC3 · 7-benzyl-1,3-dimethyl-8-piperazin-1-yl-3,7-dihydro-purine-2,6-dione · ligand · 8 copies · chains A, C, B, D
- NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 33 copies · chains A, B, C, D
- BMA · beta-D-mannopyranose · sugar · 2 copies · chains B
- SO4 · Sulfate ion · ion · 4 copies · chains A, B, C, D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
20 pockets found on a 1 Å grid, 15 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 62 | 0.74 | 0.99 | 22 | empty |
| 2 | 542 | 0.68 | 0.78 | 59 | SC3 |
| 3 | 637 | 0.68 | 0.77 | 74 | SC3 |
| 4 | 546 | 0.68 | 0.78 | 56 | SC3 |
| 5 | 609 | 0.68 | 0.77 | 72 | SC3 |
Interfaces
4 interfaces between chains.
- A–B · 2300 Ų buried · 41 hydrogen bonds · protein-protein
- C–D · 2294 Ų buried · 39 hydrogen bonds · protein-protein
- B–D · 597 Ų buried · 10 hydrogen bonds · protein-protein
- A–C · 595 Ų buried · 11 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 24 glycan, 16 disulfide (N-glycosylation, disulfide).
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 P22411
- Elsewhere: RCSB PDB 2AJ8 · PDBe 2AJ8 · UniProt P22411
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