6AVZ: HopQ-CEACAM3 WT complex

Crystal structure of the HopQ-CEACAM3 WT complex. Determined by X-ray diffraction at 2.05 Å resolution. Released 16 May 2018.

Method: X-ray diffraction
Resolution: 2.05 Å
Organisms: Helicobacter pylori, Homo sapiens, Helicobacter pylori P12
Chains: 3
Atoms: 3,513
Mol. weight: 59.43 kDa
Ligands: CA
Released: 16 May 2018

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

Secondary structure: helices and β-sheets

6AVZ contains 19 α-helices and 30 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: 2 helices, 12 β-strands

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

Chain B: 17 helices, 18 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	1	2
β-strand	106	1	3
α-helix	110-112	3
β-strand	116-121	6	4
β-strand	127-132	6	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	1	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	242-243	2
β-strand	244	1	8
α-helix	245	1
α-helix	257-258	2
β-strand	263	1	8
β-strand	268	1	7
α-helix	269-272	4
α-helix	274-299	26
α-helix	302-304	3
α-helix	316-350	35
α-helix	388-404	17
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)
part of HopQ loop	E	protein	3	Helicobacter pylori P12

Sequence of entity 1 (B), FASTA

>6AVZ_1 HopQ (chains B)
MGSSHHHHHHSQDPVQKVKNADKVQKLSDTYEQLSRLLTNDNGTNSKTSAQAINQAVNNL
NERAKTLAGGTTNSPAYQATLLALRSVLGLWNSMGYAVICGGYTKSPGENNQKNFHYTDE
NGNGTTINCGGSTNSNGTHSSNGTNTLKADKNVSLSIEQYEKIHESYQILSKALKQAGLA
PLNSKGEKLEAHVTTSKYQQDSQTKTTTSVIDTTNDAQNLLTQAQTIVNTLKDYCPMLIA
KSSSGSGGGAATNTPSWQTAGGGKNSCETFGAEFSAASDMINNAQKIVQETQQLSANQPK
NITQPHNLNLNTPSSLTALAQKMLKNAQSQAEILKLANQVESDFNKLSSGHLKDYIGKCD
MSAISSTNMTMQSQKNNWGNGCAGVEETLTSLKTSAADFNNQTPQINQAQNLANTLIQEL
GNNPFRNMGMIASSTTNNG

Sequence of entity 2 (A), FASTA

>6AVZ_2 Carcinoembryonic antigen-related cell adhesion molecule 3 (chains A)
MAKLTIESMPLSVAEGKEVLLLVHNLPQHLFGYSWYKGERVDGNSLIVGYVIGTQQATPG
AAYSGRETIYTNASLLIQNVTQNDIGFYTLQVIKSDLVNEEATGQFHVY

Sequence of entity 3 (E), FASTA

>6AVZ_3 part of HopQ loop (chains E)
XXX

Ligands and cofactors

ID	Name	Formula	Copies
CA	Calcium ion	Ca	2

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:

6AW3 2.66 Å, Crystal structure of the HopQ-CEACAM3 L44Q complex
6AW2 2.68 Å, Crystal structure of the HopQ-CEACAM1 complex

Browse structure collections

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