Research workbench
Cryo-EM structure of human insulin degrading enzyme in complex with insulin
Analyse Cryo-EM structure of human insulin degrading enzyme in complex with insulin in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6B3Q
- Type
- protein
- Length
- 1,929 residues
- Chains
- 4
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Insulin-degrading enzyme; Insulin
- EC
- 3.4.24.56
- UniProt
- P14735, P01308
- Pockets
- 20 · best druggability 0.88
Structure
electron microscopy · 4 distinct chains · 37% helix, 16% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Insulin-degrading enzyme (EC 3.4.24.56) | protein | 948 | 37% helix, 16% strand | P14735 |
| B | Insulin-degrading enzyme (EC 3.4.24.56) | protein | 938 | 38% helix, 17% strand | P14735 |
| a | Insulin | protein | 28 | 0% helix, 4% strand | P01308 |
| b | Insulin | protein | 15 | 0% helix, 7% strand | P01308 |
Pockets
20 pockets found on a 1 Å grid, 17 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1044 | 0.88 | 0.89 | 101 | empty |
| 2 | 862 | 0.86 | 0.88 | 93 | empty |
| 3 | 591 | 0.81 | 0.86 | 67 | empty |
| 4 | 372 | 0.75 | 0.86 | 53 | empty |
| 5 | 592 | 0.75 | 0.82 | 78 | empty |
Interfaces
3 interfaces between chains.
- A–a · 1638 Ų buried · 13 hydrogen bonds · protein-protein
- A–B · 1545 Ų buried · 19 hydrogen bonds · protein-protein
- B–b · 995 Ų buried · 9 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 4 disulfide (disulfide).
Compared structures
- 6B3Q · Cryo-EM structure of human insulin degrading enzyme in complex with insulin · 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
- Every structure of UniProt P01308
- Elsewhere: RCSB PDB 6B3Q · PDBe 6B3Q · UniProt P14735 · UniProt P01308
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