Crystal structure of the DAP BII (G675R) dipeptide complex. Determined by X-ray diffraction at 2.18 Å resolution. Released 15 Jul 2015.
Explore 4Y06 in 3D Show helices and sheets RCSB PDB PDBe
4Y06 contains 87 α-helices and 50 β-strands across 2 chains. Residue ranges use author residue numbering, as in the PDB file, from PDBe. To see them in 3D, choose the Cartoon representation with Secondary structure coloring: helices, sheets and coils get different colors.
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 29 | 1 | 1 |
| α-helix | 31-33 | 3 | |
| α-helix | 34-44 | 11 | |
| α-helix | 50-54 | 5 | |
| α-helix | 61-63 | 3 | |
| β-strand | 64-66 | 3 | 2 |
| β-strand | 71-74 | 4 | 2 |
| β-strand | 80-83 | 4 | 2 |
| α-helix | 85-94 | 10 | |
| α-helix | 102-105 | 4 | |
| β-strand | 107-108 | 2 | 2 |
| α-helix | 115 | 1 | |
| β-strand | 116-117 | 2 | 2 |
| β-strand | 124-132 | 9 | 2 |
| α-helix | 134-144 | 11 | |
| α-helix | 148-167 | 20 | |
| β-strand | 172-179 | 8 | 2 |
| α-helix | 180-182 | 3 | |
| β-strand | 184-193 | 10 | 2 |
| β-strand | 195-201 | 7 | 2 |
| α-helix | 204-207 | 4 | |
| α-helix | 211-214 | 4 | |
| β-strand | 226-232 | 7 | 2 |
| β-strand | 246-247 | 2 | 2 |
| β-strand | 256 | 1 | 1 |
| α-helix | 260-261 | 2 | |
| β-strand | 266-271 | 6 | 1 |
| α-helix | 282-287 | 6 | |
| α-helix | 288-292 | 5 | |
| α-helix | 293-312 | 20 | |
| α-helix | 315-320 | 6 | |
| α-helix | 322-344 | 23 | |
| α-helix | 347-363 | 17 | |
| α-helix | 366-368 | 3 | |
| α-helix | 370-388 | 19 | |
| α-helix | 390-399 | 10 | |
| α-helix | 403-418 | 16 | |
| α-helix | 422-424 | 3 | |
| α-helix | 426 | 1 | |
| α-helix | 431-433 | 3 | |
| α-helix | 434-443 | 10 | |
| α-helix | 444-447 | 4 | |
| α-helix | 450-465 | 16 | |
| α-helix | 469-471 | 3 | |
| α-helix | 474-480 | 7 | |
| α-helix | 485-496 | 12 | |
| α-helix | 503-511 | 9 | |
| α-helix | 514-519 | 6 | |
| α-helix | 523-566 | 44 | |
| α-helix | 573-575 | 3 | |
| β-strand | 580-586 | 7 | 1 |
| β-strand | 589 | 1 | 3 |
| β-strand | 595-597 | 3 | 3 |
| β-strand | 600-602 | 3 | 1 |
| α-helix | 603-608 | 6 | |
| α-helix | 620-627 | 8 | |
| β-strand | 636 | 1 | 4 |
| β-strand | 641 | 1 | 4 |
| β-strand | 643-648 | 6 | 1 |
| α-helix | 659 | 1 | |
| β-strand | 660-662 | 3 | 1 |
| β-strand | 668-675 | 8 | 1 |
| α-helix | 677-683 | 7 | |
| α-helix | 688-690 | 3 | |
| β-strand | 693-697 | 5 | 1 |
| α-helix | 698-707 | 10 | |
| α-helix | 712-717 | 6 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 29 | 1 | 5 |
| α-helix | 31-33 | 3 | |
| α-helix | 34-44 | 11 | |
| α-helix | 50-54 | 5 | |
| α-helix | 61-63 | 3 | |
| β-strand | 64-66 | 3 | 6 |
| β-strand | 71-74 | 4 | 6 |
| β-strand | 80-83 | 4 | 6 |
| α-helix | 85-94 | 10 | |
| α-helix | 102-105 | 4 | |
| β-strand | 107-108 | 2 | 6 |
| α-helix | 112-114 | 3 | |
| α-helix | 115 | 1 | |
| β-strand | 116-117 | 2 | 6 |
| β-strand | 124-132 | 9 | 6 |
| α-helix | 134-142 | 9 | |
| α-helix | 148-166 | 19 | |
| β-strand | 172-179 | 8 | 6 |
| α-helix | 180-182 | 3 | |
| β-strand | 184-193 | 10 | 6 |
| β-strand | 195-201 | 7 | 6 |
| α-helix | 204-207 | 4 | |
| α-helix | 211-214 | 4 | |
| β-strand | 226-232 | 7 | 6 |
| β-strand | 246-247 | 2 | 6 |
| β-strand | 256 | 1 | 5 |
| α-helix | 260-261 | 2 | |
| β-strand | 266-271 | 6 | 5 |
| β-strand | 275 | 1 | 7 |
| α-helix | 282-287 | 6 | |
| α-helix | 288-292 | 5 | |
| α-helix | 293-313 | 21 | |
| α-helix | 315-320 | 6 | |
| α-helix | 322-344 | 23 | |
| α-helix | 347-363 | 17 | |
| α-helix | 366-369 | 4 | |
| α-helix | 370-388 | 19 | |
| α-helix | 390-399 | 10 | |
| α-helix | 403-418 | 16 | |
| α-helix | 422-424 | 3 | |
| α-helix | 426 | 1 | |
| α-helix | 431-433 | 3 | |
| α-helix | 434-443 | 10 | |
| α-helix | 444-446 | 3 | |
| α-helix | 450-465 | 16 | |
| α-helix | 469-471 | 3 | |
| α-helix | 474-480 | 7 | |
| α-helix | 485-495 | 11 | |
| α-helix | 503-511 | 9 | |
| α-helix | 514-519 | 6 | |
| α-helix | 523-566 | 44 | |
| α-helix | 573-575 | 3 | |
| β-strand | 576 | 1 | 7 |
| β-strand | 580-586 | 7 | 5 |
| β-strand | 589 | 1 | 3 |
| β-strand | 595-597 | 3 | 3 |
| β-strand | 600-602 | 3 | 5 |
| α-helix | 603-608 | 6 | |
| α-helix | 620-627 | 8 | |
| β-strand | 636 | 1 | 8 |
| β-strand | 641 | 1 | 8 |
| β-strand | 643-648 | 6 | 5 |
| α-helix | 659 | 1 | |
| β-strand | 660-662 | 3 | 5 |
| β-strand | 668-675 | 8 | 5 |
| α-helix | 677-683 | 7 | |
| α-helix | 688-690 | 3 | |
| β-strand | 693-697 | 5 | 5 |
| α-helix | 698-707 | 10 | |
| α-helix | 712-717 | 6 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Dipeptidyl aminopeptidase BII | A, B | protein | 722 | Pseudoxanthomonas mexicana | V5YM14 (AlphaFold model) |
>4Y06_1 Dipeptidyl aminopeptidase BII (chains A, B) MRPNLLAAAIAVPLSLLAAQIAQAGEGMWVPQQLPEIAGPLKKAGLKLSPQQISDLTGDP MGAVVALGGCTASFVSPNGLVVTNHHCAYGAIQLNSTAENNLIKNGFNAPTTADEVSAGP NARVFVLDEITDVTKDAKAAIAAAGDDALARTKALEAFEKKLIADCEAEAGFRCRLYSFS GGNTYRLFKNLEIKDVRLAYAPPGSVGKFGGDIDNWMWPRHTGDFAFYRAYVGKDGKPAA FSKDNVPYQPKHWLKFADQPLGAGDFVMVAGYPGSTNRYALAAEFDNTAQWTYPTIARHY KNQIAMVEAAGKQNADIQVKYAATMAGWNNTSKNYDGQLEGFKRIDAAGQKLREEAAVLG WLKGQGAKGQPALDAHAKLLDLLEQSKATRDRDLTLALFNNTAMLGSATQLYRLSIEREK PNAERESGYQERDLPAIEGGLKQLERRYVAAMDRQLQEYWLNEYIKLPADQRVAAVDAWL GGNDAAAVKRALDRLAGTKLGSTEERLKWFAADRKAFEASNDPAIQYAVAVMPTLLKLEQ ERKTRAGENLAARPVYLQALADYKKSQGEFVYPDANLSLRITFGNVMGYAPKDGMEYTPF TTLEGVVAKETGQDPFDSPKALLDAVAAKRYGGLEDKRIGSVPVNYLSDLDITGGNSGSP VLDAHGKLVGLAFDRNWESVSSNWVFDPKMTRMIAVDGRYLRWIMQEVYPAPQLLKEMNV GK
Water and common crystallization additives (GOL) are not listed.
Structural and mutational analyses of dipeptidyl peptidase 11 from Porphyromonas gingivalis reveal the molecular basis for strict substrate specificity. Sakamoto, Y., Suzuki, Y., Iizuka, I. et al. Sci Rep (2015) 5:11151-11151. DOI 10.1038/srep11151 · PubMed
Other PDB entries of the same protein (UniProt V5YM14 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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