2WC0
crystal structure of human insulin degrading enzyme in complex with iodinated insulin
Entity
| Entity ID | Chain ID | Description | Type | Chain length | Formula weight | Number of molecules | DB Name (Accession) | Biological source | Descriptive keywords |
| 1 | A, B (A, B) | INSULIN-DEGRADING ENZYME | polymer | 990 | 114560.6 | 2 | UniProt (P14735) Pfam (PF00675) Pfam (PF05193) Pfam (PF16187) | HOMO SAPIENS (HUMAN) | INSULIN PROTEASE, INSULYSIN, INSULINASE |
| 2 | C, E (C, E) | INSULIN A CHAIN | polymer | 21 | 2383.7 | 2 | UniProt (P01308) | HOMO SAPIENS | |
| 3 | D, F (D, F) | INSULIN B CHAIN | polymer | 30 | 3434.0 | 2 | UniProt (P01308) Pfam (PF00049) | HOMO SAPIENS | |
| 4 | G, L (A, B) | ZINC ION | non-polymer | 65.4 | 2 | Chemie (ZN) | |||
| 5 | H, I, J, K, M... (A, B) | 1,4-DIETHYLENE DIOXIDE | non-polymer | 88.1 | 8 | Chemie (DIO) | |||
| 6 | Q, R, S, T, U... (A, B, C, D, E...) | water | water | 18.0 | 360 | Chemie (HOH) |
Sequence modifications
A, B: 30 - 41 (PDB: 2WC0)
A, B: 42 - 1019 (UniProt: P14735)
A, B: 42 - 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 | 6 |
| Total formula weight | 240756.5 | |
| Non-Polymers* | Number of molecules | 10 |
| Total formula weight | 835.7 | |
| All* | Total formula weight | 241592.1 |
