6AW3: HopQ-CEACAM3 L44Q complex

Crystal structure of the HopQ-CEACAM3 L44Q complex. Determined by X-ray diffraction at 2.66 Å resolution. Released 16 May 2018.

Method: X-ray diffraction
Resolution: 2.66 Å
Organisms: Helicobacter pylori, Homo sapiens
Chains: 2
Atoms: 3,375
Mol. weight: 59.09 kDa
Released: 16 May 2018

Explore 6AW3 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

6AW3 contains 16 α-helices and 29 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: 3 helices, 12 β-strands

Element	Residues	Length	Sheet
β-strand	3-7	5	8
β-strand	10-11	2	9
β-strand	17-22	6	8
α-helix	24-25	2
β-strand	28-35	8	10
α-helix	41-43	3
β-strand	44-49	6	10
β-strand	56-57	2	10
β-strand	65-67	3	8
β-strand	73-75	3	8
α-helix	80-82	3
β-strand	84-92	9	10
β-strand	96	1	5
β-strand	97-104	8	10
β-strand	105-106	2	9

Chain B: 13 helices, 17 β-strands

Element	Residues	Length	Sheet
α-helix	53-72	20
α-helix	78-97	20
α-helix	98-100	3
β-strand	101	1	1
β-strand	103-105	3	2
β-strand	106	1	3
β-strand	116-120	5	4
β-strand	128-132	5	4
β-strand	135-136	2	5
β-strand	142-143	2	5
α-helix	147-149	3
β-strand	151	1	3
β-strand	153	1	6
β-strand	157	1	6
β-strand	158-159	2	2
α-helix	160-179	20
α-helix	182-184	3
β-strand	191-201	11	4
β-strand	207-217	11	4
α-helix	220-237	18
β-strand	240	1	7
β-strand	241	1	1
α-helix	242-245	4
β-strand	268	1	7
α-helix	269-298	30
α-helix	302-305	4
α-helix	316-351	36
β-strand	372-374	3	4
α-helix	388-403	16
α-helix	406-418	13

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
HopQ	B	protein	439	Helicobacter pylori	H6A3H4 (AlphaFold model)
Carcinoembryonic antigen-related cell adhesion molecule 3	A	protein	109	Homo sapiens	P40198 (AlphaFold model)

Sequence of entity 1 (B), FASTA

>6AW3_1 HopQ (chains B)
MGSSHHHHHHSQDPVQKVKNADKVQKLSDTYEQLSRLLTNDNGTNSKTSAQAINQAVNNL
NERAKTLAGGTTNSPAYQATLLALRSVLGLWNSMGYAVICGGYTKSPGENNQKNFHYTDE
NGNGTTINCGGSTNSNGTHSSNGTNTLKADKNVSLSIEQYEKIHESYQILSKALKQAGLA
PLNSKGEKLEAHVTTSKYQQDSQTKTTTSVIDTTNDAQNLLTQAQTIVNTLKDYCPMLIA
KSSSGSGGGAATNTPSWQTAGGGKNSCETFGAEFSAASDMINNAQKIVQETQQLSANQPK
NITQPHNLNLNTPSSLTALAQKMLKNAQSQAEILKLANQVESDFNKLSSGHLKDYIGKCD
MSAISSTNMTMQSQKNNWGNGCAGVEETLTSLKTSAADFNNQTPQINQAQNLANTLIQEL
GNNPFRNMGMIASSTTNNG

Sequence of entity 2 (A), FASTA

>6AW3_2 Carcinoembryonic antigen-related cell adhesion molecule 3 (chains A)
MAKLTIESMPLSVAEGKEVLLLVHNLPQHLFGYSWYKGERVDGNSQIVGYVIGTQQATPG
AAYSGRETIYTNASLLIQNVTQNDIGFYTLQVIKSDLVNEEATGQFHVY

Primary citation

TheHelicobacter pyloriadhesin protein HopQ exploits the dimer interface of human CEACAMs to facilitate translocation of the oncoprotein CagA. Bonsor, D.A., Zhao, Q., Schmidinger, B. et al. EMBO J (2018) 37. DOI 10.15252/embj.201798664 · PubMed

Other PDB entries of the same protein (UniProt H6A3H4 (AlphaFold model), which also has an AlphaFold model), best resolution first:

6AVZ 2.05 Å, Crystal structure of the HopQ-CEACAM3 WT complex
6AW2 2.68 Å, Crystal structure of the HopQ-CEACAM1 complex

Browse structure collections

About this viewer

MolViewer shows 6AW3 directly in your browser with nothing to install. Switch between cartoon, ball-and-stick, spacefill and surface views, color by chain, secondary structure or B-factor, measure distances, angles and dihedrals, and share or embed the view.