6XNW: V39A mutant of human CEACAM1

Crystal structure of V39A mutant of human CEACAM1. Determined by X-ray diffraction at 1.9 Å resolution. Released 24 Mar 2021.

Method: X-ray diffraction
Resolution: 1.9 Å
Organism: Homo sapiens
Chains: 4
Atoms: 3,373
Mol. weight: 47.6 kDa
Ligands: NI
Released: 24 Mar 2021

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

Secondary structure: helices and β-sheets

6XNW contains 10 α-helices and 44 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.

Chains A and B: 3 helices, 11 β-strands

Element	Residues	Length	Sheet
β-strand	3-7	5	1
β-strand	10-11	2	2
β-strand	17-22	6	1
α-helix	24-25	2
β-strand	28-35	8	3
α-helix	41-43	3
β-strand	44-49	6	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	98-104	7	3
β-strand	105-106	2	2

Chain C: 2 helices, 11 β-strands

Element	Residues	Length	Sheet
β-strand	3-7	5	7
β-strand	10-11	2	8
β-strand	17-22	6	7
β-strand	28-35	8	9
α-helix	41-43	3
β-strand	44-48	5	9
β-strand	55-57	3	9
β-strand	65-67	3	7
β-strand	73-75	3	7
α-helix	80-82	3
β-strand	84-92	9	9
β-strand	97-104	8	9
β-strand	105-106	2	8

Chain D: 2 helices, 11 β-strands

Element	Residues	Length	Sheet
β-strand	3-7	5	10
β-strand	10-11	2	11
β-strand	17-22	6	10
β-strand	28-35	8	12
α-helix	41-43	3
β-strand	44-49	6	12
β-strand	54-57	4	12
β-strand	65-67	3	10
β-strand	73-75	3	10
α-helix	80-82	3
β-strand	84-92	9	12
β-strand	97-104	8	12
β-strand	105-106	2	11

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Carcinoembryonic antigen-related cell adhesion molecule 1	A, B, C, D	protein	107	Homo sapiens	P13688 (AlphaFold model)

Sequence of entity 1 (A, B, C, D), FASTA

>6XNW_1 Carcinoembryonic antigen-related cell adhesion molecule 1 (chains A, B, C, D)
QLTTESMPFNVAEGKEVLLLVHNLPQQLFGYSWYKGERADGNRQIVGYAIGTQQATPGPA
NSGRETIYPNASLLIQNVTQNDTGFYTLQVIKSDLVNEEATGQFHVY

Ligands and cofactors

ID	Name	Formula	Copies
NI	Nickel (II) ion	Ni	2

Primary citation

Structural basis of the dynamic human CEACAM1 monomer-dimer equilibrium. Gandhi, A.K., Sun, Z.J., Kim, W.M. et al. Commun Biol (2021) 4:360-360. DOI 10.1038/s42003-021-01871-2 · 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
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
9GH5 2.7 Å, Complex of Fusobacterium nucleatum CbpF with human CEACAM1

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