1FF5: E-cadherin double domain

Structure of E-cadherin double domain. Determined by X-ray diffraction at 2.93 Å resolution. Released 23 Aug 2000.

Method: X-ray diffraction
Resolution: 2.93 Å
Organism: Mus musculus
Chains: 2
Atoms: 3,633
Mol. weight: 48.08 kDa
Ligands: CA
Released: 23 Aug 2000

Explore 1FF5 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

1FF5 contains 7 α-helices and 37 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: 4 helices, 19 β-strands

Element	Residues	Length	Sheet
α-helix	5-6	2
β-strand	7-10	4	1
β-strand	19-23	5	2
α-helix	27-30	4
β-strand	34-39	6	1
β-strand	41	1	3
β-strand	45	1	3
β-strand	51-54	4	2
β-strand	59-62	4	2
β-strand	73-82	10	1
β-strand	87	1	1
β-strand	92-99	8	1
α-helix	100	1
β-strand	107-108	2	4
β-strand	112-118	7	5
α-helix	121-122	2
β-strand	126-129	4	6
β-strand	132-133	2	4
β-strand	147-152	6	5
β-strand	163-165	3	6
β-strand	171-174	4	6
β-strand	186-194	9	5
β-strand	202-212	11	5

Chain B: 3 helices, 18 β-strands

Element	Residues	Length	Sheet
α-helix	5-6	2
β-strand	7-10	4	7
β-strand	19-23	5	8
α-helix	28-30	3
β-strand	34-39	6	7
β-strand	41	1	9
β-strand	45	1	9
β-strand	51-54	4	8
β-strand	59-62	4	8
β-strand	73-82	10	7
β-strand	86-99	14	7
β-strand	107-108	2	10
β-strand	112-118	7	11
α-helix	121-122	2
β-strand	126-129	4	12
β-strand	132-133	2	10
β-strand	147-152	6	11
β-strand	163-165	3	12
β-strand	171-174	4	12
β-strand	186-194	9	11
β-strand	202-212	11	11

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Epithelial cadherin	A, B	protein	219	Mus musculus	P09803 (AlphaFold model)

Sequence of entity 1 (A, B), FASTA

>1FF5_1 EPITHELIAL CADHERIN (chains A, B)
MDWVIPPISCPENEKGEFPKNLVQIKSNRDKETKVFYSITGQGADKPPVGVFIIERETGW
LKVTQPLDREAIAKYILYSHAVSSNGEAVEDPMEIVITVTDQNDNRPEFTQEVFEGSVAE
GAVPGTSVMKVSATDADDDVNTYNAAIAYTIVSQDPELPHKNMFTVNRDTGVISVLTSGL
DRESYPTYTLVVQAADLQGEGLSTTAKAVITVKDINDNA

Ligands and cofactors

ID	Name	Formula	Copies
CA	Calcium ion	Ca	6

Primary citation

A new crystal structure, Ca2+ dependence and mutational analysis reveal molecular details of E-cadherin homoassociation. Pertz, O., Bozic, D., Koch, A.W. et al. EMBO J (1999) 18:1738-1747. DOI 10.1093/emboj/18.7.1738 · PubMed

Other PDB entries of the same protein (UniProt P09803 (AlphaFold model), which also has an AlphaFold model), best resolution first:

3QRB 1.8 Å, crystal structure of E-cadherin EC1-2 P5A P6A
2OMW 1.85 Å, Crystal structure of InlA S192N Y369S/mEC1 complex
1EDH 2.0 Å, E-cadherin domains 1 and 2 in complex with calcium
1I7W 2.0 Å, Beta-catenin/phosphorylated E-cadherin complex
3LNE 2.0 Å, Crystal structure of E-cadherin EC12 K14E
3LNI 2.3 Å, Crystal structure of E-cadherin EC12 E89A
2QVF 2.4 Å, mouse E-cadherin domains 1,2
4QD2 2.4 Å, Molecular basis for disruption of E-cadherin adhesion by botulinum neurotoxin A complex
3LNF 2.5 Å, Crystal structure of E-cadherin EC12 K14EW2A
3LNH 2.6 Å, Crystal structure of E-cadherin EC12 W2A
7AR4 2.6 Å, Crystal structure of beta-catenin in complex with cyclic peptide inhibitor
3LNG 2.7 Å, Crystal structure of E-cadherin EC12 AA extension

Browse structure collections

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