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The structure of cysteine-free human insulin degrading enzyme

Analyse The structure of cysteine-free human insulin degrading enzyme in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3QZ2
Type: protein
Length: 1,905 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: ZN
Pockets: 20 · best druggability 0.85

Structure

x-ray diffraction · 2 distinct chains · 44% helix, 20% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Insulin-degrading enzyme (EC 3.4.24.56)	protein	953	44% helix, 20% strand	P14735
B	Insulin-degrading enzyme (EC 3.4.24.56)	protein	952	44% helix, 20% strand	P14735

Ligands and binding sites

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.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	839	0.85	0.87	92	empty
2	1048	0.76	0.79	121	empty
3	461	0.72	0.82	71	empty
4	438	0.68	0.80	72	empty
5	358	0.65	0.80	37	ZN

Interfaces

1 interface between chains.

A–B · 1529 Å² buried · 12 hydrogen bonds · protein-protein

Compared structures

3QZ2 · The structure of cysteine-free human insulin degrading enzyme · 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 3QZ2 · PDBe 3QZ2 · UniProt P14735

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