Cyclic Peptide DataBank (CPDB)
Browse and visualize 3D structures of polypeptides
Browse and visualize 3D structures of polypeptides
| PDB ID | 2WBY Go to RCSB ➚ |
| Title | Crystal structure of human insulin-degrading enzyme in complex with insulin |
| Method | X-RAY DIFFRACTION |
| Resolution | 2.60 Å |
| R-factors | R-work: 0.164, R-free: 0.218 |
| Release Date | 2009-03-24 |
| Authors | Manolopoulou, M.; Guo, Q.; Malito, E.; Schilling, A.B.; Tang, W.J. |
| Source Organism | HOMO SAPIENS |
| Expression Host | Escherichia coli BL21(DE3) |
| Keywords | HYDROLASE/HORMONE, GLUCOSE METABOLISM, CARBOHYDRATE METABOLISM, DISEASE MUTATION, DIABETES MELLITUS, ZINC, DIOXANE, INSULIN, HORMONE, SECRETED, PROTEASE, DISULFIDE BOND, PHARMACEUTICAL, METALLOPROTEASE, HUMAN INSULIN-DEGRADNG ENZYME, HYDROLASE, CYTOPLASM, POLYMORPHISM, METAL-BINDING, CLEAVAGE ON PAIR OF BASIC RESIDUES, HYDROLASE-HORMONE complex |
| EC Number | 3.4.24.56 |
| Molecular Weight | 238.09 kDa |
| Entity Count | Protein: 3, Nucleic Acid: 0, NA Hybrid: 0 |
| Space Group | P 65 |
| Cell Parameters | a=262.32 Å, b=262.32 Å, c=90.61 Å, α=90.00°, β=90.00°, γ=120.00° |
| Disulfide Bond | C6-C11;E6-E11 |
| Other Links | Yes |
| Peptide Chains | C, D, E, F |
| Protein Chains | A, B |
| Peptide Lengths | 20, 19 |
| Protein Lengths | 990 |
| 1 | MHHHHHHAAG IPMNNPAIKR IGNHITKSPE DKREYRGLEL ANGIKVLLIS DPTTDKSSAA |
| 61 | LDVHIGSLSD PPNIAGLSHF LQHMLFLGTK KYPKENEYSQ FLSEHAGSSN AFTSGEHTNY |
| 121 | YFDVSHEHLE GALDRFAQFF LSPLFDESAK DREVNAVDSE HEKNVMNDAW RLFQLEKATG |
| 181 | NPKHPFSKFG TGNKYTLETR PNQEGIDVRQ ELLKFHSAYY SSNLMAVVVL GRESLDDLTN |
| 241 | LVVKLFSEVE NKNVPLPEFP EHPFQEEHLK QLYKIVPIKD IRNLYVTFPI PDLQKYYKSN |
| 301 | PGHYLGHLIG HEGPGSLLSE LKSKGWVNTL VGGQKEGARG FMFFIINVDL TEEGLLHVED |
| 361 | IILHMFQYIQ KLRAEGPQEW VFQELKDLNA VAFRFKDKER PRGYTSKIAG ILHYYPLEEV |
| 421 | LTAEYLLEEF RPDLIEMVLD KLRPENVRVA IVSKSFEGKT DRTEEWYGTQ YKQEAIPDEV |
| 481 | IKKWQNADLN GKFKLPTKNE FIPTNFEILP LEKEATPYPA LIKDTAMSKL WFKQDDKFFL |
| 541 | PKANLNFEFF SPFAYVDPLH SNMAYLYLEL LKDSLNEYAY AAELAGLSYD LQNTIYGMYL |
| 601 | SVKGYNDKQP ILLKKIIEKM ATFEIDEKRF EIIKEAYMRS LNNFRAEQPH QHAMYYLRLL |
| 661 | MTEVAWTKDE LKEALDDVTL PRLKAFIPQL LSRLHIEALL HGNITKQAAL GIMQMVEDTL |
| 721 | IEHAHTKPLL PSQLVRYREV QLPDRGWFVY QQRNEVHNNS GIEIYYQTDM QSTSENMFLE |
| 781 | LFAQIISEPA FNTLRTKEQL GYIVFSGPRR ANGIQGLRFI IQSEKPPHYL ESRVEAFLIT |
| 841 | MEKSIEDMTE EAFQKHIQAL AIRRLDKPKK LSAESAKYWG EIISQQYNFD RDNTEVAYLK |
| 901 | TLTKEDIIKF YKEMLAVDAP RRHKVSVHVL AREMDSNPVV GEFPAQNDIN LSQAPALPQP |
| 961 | EVIQNMTEFK RGLPLFPLVK PHINFMAAKL |
| 1 | GIVEQCCTSI CSLYQLENYC |
| 1 | FVNQHLCGSH LVEALYLVC |
Molecular Basis of Catalytic Chamber-Assisted Unfolding and Cleavage of Human Insulin by Human Insulin Degrading Enzyme.
J Biological Chem, 2009
| ID | Name | Formula | Molecular Weight |
|---|---|---|---|
| ZN | ZINC ION | Zn | 65.409 |
Assembly ID: 1
Details: author_and_software_defined_assembly
Oligomeric State: Hetero 3-mer
Stoichiometry: A1, B1, C1
Assembly ID: 2
Details: author_and_software_defined_assembly
Oligomeric State: Hetero 3-mer
Stoichiometry: A1, B1, C1