Research workbench
Structure of human DPP3 in complex with a hydroxyethylene transition state peptidomimetic
Analyse Structure of human DPP3 in complex with a hydroxyethylene transition state… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7OUP
- Type
- protein
- Length
- 727 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- Q9NY33
- Ligands
- 1QI, ZN, K, MG
Structure
x-ray diffraction · 2 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 724 | — | Q9NY33 |
| F | — | protein | 3 | — | — |
Ligands and binding sites
- 1QI · (2R,4S,5S)-5-azanyl-6-methyl-4-oxidanyl-2-(phenylmethyl)heptanoic acid · ligand · chains A, F
- ZN · Zinc ion · metal · chains A
- K · Potassium ion · metal · chains A
- MG · Magnesium ion · metal · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 7OUP · Structure of human DPP3 in complex with a hydroxyethylene transition state peptidomimetic · the same entry in another collection · chain A against A, TM-score 1.00
- Q9NY33 · AlphaFold monomer V2.0 prediction for dipeptidyl peptidase 3 (Q9NY33) · a predicted model of the same protein · 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 Q9NY33
- Elsewhere: RCSB PDB 7OUP · PDBe 7OUP · UniProt Q9NY33
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