4CFQ: Protein S100-A4

Ca-bound truncated (delta13C) and C3S, C81S and C86S mutated S100A4 complexed with non-muscle myosin IIA. Determined by X-ray diffraction at 1.37 Å resolution. Released 7 May 2014.

Method: X-ray diffraction
Resolution: 1.37 Å
Organism: HOMO SAPIENS
Chains: 6
Atoms: 3,476
Mol. weight: 52.52 kDa
Ligands: CA
Released: 7 May 2014

Explore 4CFQ in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

4CFQ contains 22 α-helices and 10 β-strands across 6 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: 5 helices, 2 β-strands

Element	Residues	Length	Sheet
α-helix	4-20	17
β-strand	28-29	2	1
α-helix	31-41	11
α-helix	43-45	3
α-helix	52-62	11
β-strand	70-71	2	1
α-helix	72-86	15

Chain B: 5 helices, 2 β-strands

Element	Residues	Length	Sheet
α-helix	4-20	17
β-strand	29	1	2
α-helix	31-41	11
α-helix	43-45	3
α-helix	52-62	11
β-strand	70	1	2
α-helix	72-82	11

Chain C: 5 helices, 2 β-strands

Element	Residues	Length	Sheet
α-helix	4-20	17
β-strand	28-29	2	3
α-helix	31-41	11
α-helix	43-45	3
α-helix	52-62	11
β-strand	70-71	2	3
α-helix	72-87	16

Chain D: 5 helices, 3 β-strands

Element	Residues	Length	Sheet
α-helix	4-20	17
β-strand	29	1	4
α-helix	31-41	11
α-helix	43-45	3
β-strand	46	1	5
α-helix	52-62	11
β-strand	70	1	4
α-helix	72-82	11

Chain Q: 1 helix, 0 β-strands

Element	Residues	Length	Sheet
α-helix	1904-1921	18

Chain R: 1 helix, 1 β-strand

Element	Residues	Length	Sheet
α-helix	1904-1922	19
β-strand	1929	1	5

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Protein S100-A4	A, B, C, D	protein	91	HOMO SAPIENS	P26447 (AlphaFold model)
Myosin-9	Q, R	protein	45	HOMO SAPIENS	P35579 (AlphaFold model)

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

>4CFQ_1 PROTEIN S100-A4 (chains A, B, C, D)
GSHMASPLEKALDVMVSTFHKYSGKEGDKFKLNKSELKELLTRELPSFLGKRTDEAAFQK
LMSNLDSNRDNEVDFQEYCVFLSSIAMMSNE

Sequence of entity 2 (Q, R), FASTA

>4CFQ_2 MYOSIN-9 (chains Q, R)
YRKLQRELEDATETADAMNREVSSLKNKLRRGDLPFVVPRRMARK

Ligands and cofactors

ID	Name	Formula	Copies
CA	Calcium ion	Ca	8

Primary citation

The C-Terminal Random Coil Region Tunes the Ca2+-Binding Affinity of S100A4 Through Conformational Activation. Duelli, A., Kiss, B., Lundholm, I. et al. PLoS One (2014) 9:97654. DOI 10.1371/JOURNAL.PONE.0097654 · PubMed

Other PDB entries of the same protein (UniProt P26447 (AlphaFold model), which also has an AlphaFold model), best resolution first:

4CFR 1.4 Å, Ca-bound S100A4 C3S, C81S, C86S and F45W mutant complexed with non- muscle myosin IIA
3C1V 1.5 Å, The 1.5 A Crystal structure of Ca2+-bound S100A4
4ETO 1.54 Å, Structure of S100A4 in complex with non-muscle myosin-IIA peptide
2Q91 1.63 Å, Structure of the Ca2+-Bound Activated Form of the S100A4 Metastasis Factor
27UH 1.82 Å, Crystal structure of a de novo-designed VHH targeting S100A4
7PSQ 1.91 Å, Crystal structure of S100A4 labeled with NU074381b.
3ZWH 1.94 Å, Ca2+-bound S100A4 C3S, C81S, C86S and F45W mutant complexed with myosin IIA
3CGA 2.03 Å, Crystal structure of metastasis-associated protein S100A4 in the active, calcium-bound…
5LPU 2.1 Å, Crystal structure of Annexin A2 complexed with S100A4
4HSZ 2.25 Å, Structure of truncated (delta8C) S100A4
3KO0 2.3 Å, Structure of the tfp-ca2+-bound activated form of the s100a4 Metastasis factor
7PSP 2.61 Å, Crystal structure of S100A4 labeled with NU000846b.

Browse structure collections

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