4Y06: DAP BII (G675R) dipeptide complex

Crystal structure of the DAP BII (G675R) dipeptide complex. Determined by X-ray diffraction at 2.18 Å resolution. Released 15 Jul 2015.

Method
X-ray diffraction
Resolution
2.18 Å
Organism
Pseudoxanthomonas mexicana
Chains
2
Atoms
11,405
Mol. weight
159.95 kDa
Ligands
ZN, GLU, LEU
Released
15 Jul 2015

Explore 4Y06 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

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.

Chain A: 43 helices, 24 β-strands

ElementResiduesLengthSheet
β-strand2911
α-helix31-333
α-helix34-4411
α-helix50-545
α-helix61-633
β-strand64-6632
β-strand71-7442
β-strand80-8342
α-helix85-9410
α-helix102-1054
β-strand107-10822
α-helix1151
β-strand116-11722
β-strand124-13292
α-helix134-14411
α-helix148-16720
β-strand172-17982
α-helix180-1823
β-strand184-193102
β-strand195-20172
α-helix204-2074
α-helix211-2144
β-strand226-23272
β-strand246-24722
β-strand25611
α-helix260-2612
β-strand266-27161
α-helix282-2876
α-helix288-2925
α-helix293-31220
α-helix315-3206
α-helix322-34423
α-helix347-36317
α-helix366-3683
α-helix370-38819
α-helix390-39910
α-helix403-41816
α-helix422-4243
α-helix4261
α-helix431-4333
α-helix434-44310
α-helix444-4474
α-helix450-46516
α-helix469-4713
α-helix474-4807
α-helix485-49612
α-helix503-5119
α-helix514-5196
α-helix523-56644
α-helix573-5753
β-strand580-58671
β-strand58913
β-strand595-59733
β-strand600-60231
α-helix603-6086
α-helix620-6278
β-strand63614
β-strand64114
β-strand643-64861
α-helix6591
β-strand660-66231
β-strand668-67581
α-helix677-6837
α-helix688-6903
β-strand693-69751
α-helix698-70710
α-helix712-7176
Chain B: 44 helices, 26 β-strands
ElementResiduesLengthSheet
β-strand2915
α-helix31-333
α-helix34-4411
α-helix50-545
α-helix61-633
β-strand64-6636
β-strand71-7446
β-strand80-8346
α-helix85-9410
α-helix102-1054
β-strand107-10826
α-helix112-1143
α-helix1151
β-strand116-11726
β-strand124-13296
α-helix134-1429
α-helix148-16619
β-strand172-17986
α-helix180-1823
β-strand184-193106
β-strand195-20176
α-helix204-2074
α-helix211-2144
β-strand226-23276
β-strand246-24726
β-strand25615
α-helix260-2612
β-strand266-27165
β-strand27517
α-helix282-2876
α-helix288-2925
α-helix293-31321
α-helix315-3206
α-helix322-34423
α-helix347-36317
α-helix366-3694
α-helix370-38819
α-helix390-39910
α-helix403-41816
α-helix422-4243
α-helix4261
α-helix431-4333
α-helix434-44310
α-helix444-4463
α-helix450-46516
α-helix469-4713
α-helix474-4807
α-helix485-49511
α-helix503-5119
α-helix514-5196
α-helix523-56644
α-helix573-5753
β-strand57617
β-strand580-58675
β-strand58913
β-strand595-59733
β-strand600-60235
α-helix603-6086
α-helix620-6278
β-strand63618
β-strand64118
β-strand643-64865
α-helix6591
β-strand660-66235
β-strand668-67585
α-helix677-6837
α-helix688-6903
β-strand693-69755
α-helix698-70710
α-helix712-7176

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Dipeptidyl aminopeptidase BIIA, Bprotein722Pseudoxanthomonas mexicanaV5YM14 (AlphaFold model)
Sequence of entity 1 (A, B), FASTA
>4Y06_1 Dipeptidyl aminopeptidase BII (chains A, B)
MRPNLLAAAIAVPLSLLAAQIAQAGEGMWVPQQLPEIAGPLKKAGLKLSPQQISDLTGDP
MGAVVALGGCTASFVSPNGLVVTNHHCAYGAIQLNSTAENNLIKNGFNAPTTADEVSAGP
NARVFVLDEITDVTKDAKAAIAAAGDDALARTKALEAFEKKLIADCEAEAGFRCRLYSFS
GGNTYRLFKNLEIKDVRLAYAPPGSVGKFGGDIDNWMWPRHTGDFAFYRAYVGKDGKPAA
FSKDNVPYQPKHWLKFADQPLGAGDFVMVAGYPGSTNRYALAAEFDNTAQWTYPTIARHY
KNQIAMVEAAGKQNADIQVKYAATMAGWNNTSKNYDGQLEGFKRIDAAGQKLREEAAVLG
WLKGQGAKGQPALDAHAKLLDLLEQSKATRDRDLTLALFNNTAMLGSATQLYRLSIEREK
PNAERESGYQERDLPAIEGGLKQLERRYVAAMDRQLQEYWLNEYIKLPADQRVAAVDAWL
GGNDAAAVKRALDRLAGTKLGSTEERLKWFAADRKAFEASNDPAIQYAVAVMPTLLKLEQ
ERKTRAGENLAARPVYLQALADYKKSQGEFVYPDANLSLRITFGNVMGYAPKDGMEYTPF
TTLEGVVAKETGQDPFDSPKALLDAVAAKRYGGLEDKRIGSVPVNYLSDLDITGGNSGSP
VLDAHGKLVGLAFDRNWESVSSNWVFDPKMTRMIAVDGRYLRWIMQEVYPAPQLLKEMNV
GK

Ligands and cofactors

IDNameFormulaCopies
ZNZinc ionZn5
GLUGlutamic acidC5 H9 N O42
LEULeucineC6 H13 N O22

Water and common crystallization additives (GOL) are not listed.

Primary citation

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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