6BYZ
Structure of Cysteine-free Human Insulin-Degrading Enzyme in complex with Substrate-selective Macrocyclic Inhibitor 37
Entity
Entity ID | Chain ID | Description | Type | Chain length | Formula weight | Number of molecules | DB Name (Accession) | Biological source | Descriptive keywords |
1 | A, B | Insulin-degrading enzyme | polymer | 1019 | 117968.7 | 2 | UniProt (P14735) Pfam (PF00675) Pfam (PF05193) Pfam (PF16187) In PDB | Homo sapiens (Human) | Abeta-degrading protease,Insulin protease,Insulinase,Insulysin |
2 | D, E | ALA-ALA-ALA | polymer | 3 | 231.2 | 2 | Escherichia coli BL21(DE3) | ||
3 | A, B | [(8R,9S,10S)-9-(2',3'-dimethyl[1,1'-biphenyl]-4-yl)-6-{[2-(trifluoromethyl)phenyl]sulfonyl}-1,6-diazabicyclo[6.2.0]decan-10-yl]methanol | non-polymer | 558.7 | 2 | Chemie (J18) | |||
4 | A, B | 4-(2-HYDROXYETHYL)-1-PIPERAZINE ETHANESULFONIC ACID | non-polymer | 238.3 | 2 | Chemie (EPE) | |||
5 | water | water | 18.0 | 389 | Chemie (HOH) |
Sequence modifications
A, B: 1 - 1019 (UniProt: P14735)
PDB | External Database | Details |
---|---|---|
Leu 110 | Cys 110 | engineered mutation |
Gln 111 | Glu 111 | engineered mutation |
Ser 171 | Cys 171 | engineered mutation |
Ala 178 | Cys 178 | engineered mutation |
Val 257 | Cys 257 | engineered mutation |
Leu 414 | Cys 414 | engineered mutation |
Asn 573 | Cys 573 | engineered mutation |
Ser 590 | Cys 590 | engineered mutation |
Ser 789 | Cys 789 | engineered mutation |
Ala 812 | Cys 812 | engineered mutation |
Ala 819 | Cys 819 | engineered mutation |
Ser 904 | Cys 904 | engineered mutation |
Asn 966 | Cys 966 | engineered mutation |
Ala 974 | Cys 974 | engineered mutation |
Sequence viewer
Contents of the asymmetric unit
Polymers | Number of chains | 4 |
Total formula weight | 236399.8 | |
Non-Polymers* | Number of molecules | 4 |
Total formula weight | 1593.9 | |
All* | Total formula weight | 237993.7 |