Helicobacter pylori adhesin HopQ type II bound to the N-terminal domain of human CEACAM1. Determined by X-ray diffraction at 2.59 Å resolution. Released 27 Jun 2018.
Explore 6GBH in 3D Show helices and sheets RCSB PDB PDBe
6GBH contains 27 α-helices and 45 β-strands across 4 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 |
|---|---|---|---|
| α-helix | 60-75 | 16 | |
| α-helix | 82-101 | 20 | |
| α-helix | 102-104 | 3 | |
| β-strand | 105 | 1 | 11 |
| β-strand | 107 | 1 | 12 |
| β-strand | 110 | 1 | 13 |
| β-strand | 120-123 | 4 | 14 |
| β-strand | 132-135 | 4 | 14 |
| α-helix | 138-141 | 4 | |
| β-strand | 143 | 1 | 13 |
| β-strand | 145 | 1 | 15 |
| β-strand | 149 | 1 | 15 |
| β-strand | 150 | 1 | 12 |
| α-helix | 152-171 | 20 | |
| β-strand | 182-191 | 10 | 14 |
| β-strand | 208-217 | 10 | 14 |
| α-helix | 220-237 | 18 | |
| β-strand | 241 | 1 | 11 |
| α-helix | 267-296 | 30 | |
| α-helix | 321-349 | 29 | |
| α-helix | 355-357 | 3 | |
| α-helix | 370-372 | 3 | |
| α-helix | 380-395 | 16 | |
| α-helix | 398-411 | 14 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 3-7 | 5 | 1 |
| β-strand | 10-12 | 3 | 2 |
| β-strand | 17-22 | 6 | 1 |
| β-strand | 28-35 | 8 | 3 |
| α-helix | 41-43 | 3 | |
| β-strand | 44-49 | 6 | 3 |
| α-helix | 50-52 | 3 | |
| β-strand | 54-57 | 4 | 3 |
| β-strand | 65-67 | 3 | 1 |
| β-strand | 73-75 | 3 | 1 |
| α-helix | 80-82 | 3 | |
| β-strand | 84-92 | 9 | 3 |
| β-strand | 97-104 | 8 | 3 |
| β-strand | 105-107 | 3 | 2 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 60-76 | 17 | |
| α-helix | 82-102 | 21 | |
| β-strand | 105 | 1 | 7 |
| β-strand | 107 | 1 | 8 |
| β-strand | 110 | 1 | 9 |
| β-strand | 121-123 | 3 | 10 |
| β-strand | 132-134 | 3 | 10 |
| α-helix | 137-141 | 5 | |
| β-strand | 143 | 1 | 9 |
| β-strand | 150 | 1 | 8 |
| α-helix | 152-171 | 20 | |
| α-helix | 173-175 | 3 | |
| β-strand | 182-191 | 10 | 10 |
| β-strand | 208-217 | 10 | 10 |
| α-helix | 220-237 | 18 | |
| β-strand | 240-241 | 2 | 7 |
| β-strand | 265-266 | 2 | 7 |
| α-helix | 267-296 | 30 | |
| α-helix | 318-348 | 31 | |
| α-helix | 380-395 | 16 | |
| α-helix | 398-409 | 12 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 3-7 | 5 | 4 |
| β-strand | 10 | 1 | 5 |
| β-strand | 17-22 | 6 | 4 |
| β-strand | 28-35 | 8 | 6 |
| α-helix | 41-43 | 3 | |
| β-strand | 44-49 | 6 | 6 |
| β-strand | 54-57 | 4 | 6 |
| β-strand | 65-67 | 3 | 4 |
| β-strand | 73-75 | 3 | 4 |
| α-helix | 80-82 | 3 | |
| β-strand | 84-92 | 9 | 6 |
| β-strand | 97-104 | 8 | 6 |
| β-strand | 105 | 1 | 5 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Carcinoembryonic antigen-related cell adhesion molecule 1 | B, D | protein | 115 | Homo sapiens | P13688 (AlphaFold model) |
| HopQ | A, C | protein | 425 | Helicobacter pylori | Q8GDI6 (AlphaFold model) |
>6GBH_1 Carcinoembryonic antigen-related cell adhesion molecule 1 (chains B, D) MQLTTESMPFNVAEGKEVLLLVHNLPQQLFGYSWYKGERVDGNRQIVGYAIGTQQATPGP ANSGRETIYPNASLLIQNVTQNDTGFYTLQVIKSDLVNEEATGQFHVYPHHHHHH
>6GBH_2 HopQ (chains A, C) MAVQKVKNADKVQKLSDAYENLNKLLANHSHSNPEAINANSATAINQAIGNLNANTQNLI DKTDNSPAYQATLLALKSTVGLWNSIAYAVICGGYTDKPNHNTTETFYNQPGQGSDSITC GGHVGLLQAGKNNSLSIEQFATLNKAYQIIQAALKQGLPALSDTKKTVEVTIKTATNANN INVNNNNNNAADTTVSITDTFINDAQNLLTQAQTIINTLQDNCPQLKGKSSSNGGTNGAN TPSWQTGANQNSCSVFGTEFSAISDMISNAQNIVQETQQLNTTPLKSIAQPNNFNLNSPN SIALAQSMLKNAQSQAAVLKLANQVGSDFNRISTGVLKNYIEECNANASSESVSSNTWGK GCAGVKQTLTSLENSNASFSSQTPQINQAQNLANTIVQELGHNPFKRVGIISSQTNNGAH HHHHH
Helicobacter pyloriadhesin HopQ disruptstransdimerization in human CEACAMs. Moonens, K., Hamway, Y., Neddermann, M. et al. EMBO J (2018) 37. DOI 10.15252/embj.201798665 · PubMed
Other PDB entries of the same protein (UniProt P13688 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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