9GH6: PDB entry 9GH6

CEACAM1 (35-234), focused refinement in the complex with CbpF. Determined by electron microscopy at 3.0 Å resolution. Released 2 Apr 2025.

Method: Electron microscopy
Resolution: 3.0 Å
Organism: Homo sapiens
Chains: 1
Atoms: 1,661
Mol. weight: 49.47 kDa
Ligands: NAG
Released: 2 Apr 2025

Explore 9GH6 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

9GH6 contains 5 α-helices and 20 β-strands across 1 chain. 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 D: 5 helices, 20 β-strands

Element	Residues	Length	Sheet
β-strand	37-41	5	1
β-strand	44-46	3	2
β-strand	51-56	6	1
β-strand	62-69	8	3
α-helix	75-77	3
β-strand	78-83	6	3
β-strand	88-91	4	3
β-strand	99-101	3	1
β-strand	107-109	3	1
α-helix	114-116	3
β-strand	118-126	9	3
β-strand	131-138	8	3
β-strand	139-141	3	2
α-helix	144-146	3
β-strand	149-151	3	4
β-strand	164-167	4	4
β-strand	175-180	6	5
β-strand	183-184	2	5
β-strand	191-194	4	4
β-strand	199-202	4	4
α-helix	207-209	3
β-strand	213-218	6	5
β-strand	223-225	3	5
α-helix	227-228	2
β-strand	229	1	5

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Carcinoembryonic antigen-related cell adhesion molecule 1	D	protein	434	Homo sapiens	P13688 (AlphaFold model)

Sequence of entity 1 (D), FASTA

>9GH6_1 Carcinoembryonic antigen-related cell adhesion molecule 1 (chains D)
MGHLSAPLHRVRVPWQGLLLTASLLTFWNPPTTAQLTTESMPFNVAEGKEVLLLVHNLPQ
QLFGYSWYKGERVDGNRQIVGYAIGTQQATPGPANSGRETIYPNASLLIQNVTQNDTGFY
TLQVIKSDLVNEEATGQFHVYPELPKPSISSNNSNPVEDKDAVAFTCEPETQDTTYLWWI
NNQSLPVSPRLQLSNGNRTLTLLSVTRNDTGPYECEIQNPVSANRSDPVTLNVTYGPDTP
TISPSDTYYRPGANLSLSCYAASNPPAQYSWLINGTFQQSTQELFIPNITVNNSGSYTCH
ANNSVTGCNRTTVKTIIVTELSPVVAKPQIKASKTTVTGDKDSVNLTCSTNDTGISIRWF
FKNQSLPSSERMKLSQGNTTLSINPVKREDAGTYWCEVFNPISKNQSDPIMLNVNYNALP
QENGLSPGHHHHHH

Ligands and cofactors

ID	Name	Formula	Copies
NAG	2-acetamido-2-deoxy-beta-D-glucopyranose	C8 H15 N O6	7

Primary citation

Structural basis for immune cell binding of Fusobacterium nucleatum via the trimeric autotransporter adhesin CbpF. Marongiu, G.L., Fink, U., Schopf, F. et al. Proc Natl Acad Sci U S A (2025) 122:e2418155122-e2418155122. DOI 10.1073/pnas.2418155122 · PubMed

Other PDB entries of the same protein (UniProt P13688 (AlphaFold model), which also has an AlphaFold model), best resolution first:

7MU8 1.7 Å, Structure of the minimally glycosylated human CEACAM1 N-terminal domain
6XO1 1.76 Å, Crystal structure of N97A mutant of human CEACAM1
23VF 1.79 Å, Crystal structure of CEACAM1 in complex with MG1124 antibody
6XNO 1.9 Å, Crystal structure of E99A mutant of human CEACAM1
6XNW 1.9 Å, Crystal structure of V39A mutant of human CEACAM1
4QXW 2.04 Å, Crystal structure of the human CEACAM1 membrane distal amino terminal (N)-domain
9U94 2.11 Å, Cryo-EM structure of Fusobacterium nucleatum CbpF in complex with human CEACAM1
2GK2 2.2 Å, Crystal structure of the N terminal domain of human CEACAM1
7RPP 2.2 Å, Crystal structure of human CEACAM1 with GFCC' and ABED face
4WHD 2.5 Å, Human CEACAM1 N-domain homodimer
6GBH 2.59 Å, Helicobacter pylori adhesin HopQ type II bound to the N-terminal domain of human CEACAM1
6AW2 2.68 Å, Crystal structure of the HopQ-CEACAM1 complex

Browse structure collections

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