Research workbench
Crystal structure of human insulin degrading enzyme (ide) in complex with inhibitor N-benzyl-N-(CARBOXYMETHYL)GLYCYL-L-histidine
Analyse Crystal structure of human insulin degrading enzyme (ide) in complex with… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4QIA
- Type
- protein
- Length
- 1,906 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Insulin-degrading enzyme
- EC
- 3.4.24.56
- UniProt
- P14735
- Ligands
- 33K, ZN
- Pockets
- 20 · best druggability 0.78
Structure
x-ray diffraction · 1 distinct chain · 44% helix, 21% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Insulin-degrading enzyme (EC 3.4.24.56) | protein | 953 | 44% helix, 21% strand | P14735 |
Ligands and binding sites
- 33K · N-benzyl-N-(carboxymethyl)glycyl-L-histidine · ligand · 2 copies · chains A, B
- ZN · Zinc ion · metal · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
20 pockets found on a 1 Å grid, 12 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 944 | 0.78 | 0.80 | 90 | empty |
| 2 | 1150 | 0.74 | 0.77 | 111 | empty |
| 3 | 482 | 0.71 | 0.81 | 81 | empty |
| 4 | 553 | 0.68 | 0.78 | 72 | empty |
| 5 | 313 | 0.65 | 0.81 | 31 | ZN |
Interfaces
1 interface between chains.
- A–B · 926 Ų buried · 9 hydrogen bonds · protein-protein
Compared structures
- 4QIA · Crystal structure of human insulin degrading enzyme (ide) in complex with inhibitor… · 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 P14735
- Elsewhere: RCSB PDB 4QIA · PDBe 4QIA · UniProt P14735
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