4JS0: Cell division control protein 42 homolog

Complex of Cdc42 with the CRIB-PR domain of IRSp53. Determined by X-ray diffraction at 1.9 Å resolution. Released 5 Mar 2014.

Method: X-ray diffraction
Resolution: 1.9 Å
Organism: Homo sapiens
Chains: 2
Atoms: 1,844
Mol. weight: 24.74 kDa
Ligands: GNP, PE4, MG
Released: 5 Mar 2014

Explore 4JS0 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

4JS0 contains 14 α-helices and 8 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: 11 helices, 6 β-strands

Element	Residues	Length	Sheet
β-strand	3-10	8	1
α-helix	16-25	10
β-strand	37-46	10	1
β-strand	49-58	10	1
α-helix	62-64	3
α-helix	68-71	4
β-strand	77-83	7	1
α-helix	87-92	6
α-helix	93-97	5
α-helix	98-104	7
β-strand	110-115	6	1
α-helix	117-119	3
α-helix	123-131	9
α-helix	136-138	3
α-helix	139-149	11
β-strand	154-156	3	1
α-helix	165-177	13

Chain B: 3 helices, 2 β-strands

Element	Residues	Length	Sheet
β-strand	267	1	1
α-helix	268-270	3
β-strand	271	1	1
α-helix	274-278	5
α-helix	281-286	6

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Cell division control protein 42 homolog	A	protein	178	Homo sapiens	P60953 (AlphaFold model)
Brain-specific angiogenesis inhibitor 1-associated protein 2	B	protein	32	Homo sapiens	Q9UQB8 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>4JS0_1 Cell division control protein 42 homolog (chains A)
MQTIKCVVVGDVAVGKTCLLISYTTNKFPSEYVPTVFDNYAVTVMIGGEPYTLGLFDTAG
QEDYDRLRPLSYPQTDVFLVCFSVVSPSSFENVKEKWVPEITHHCPKTPFLLVGTQIDLR
DDPSTIEKLAKNKQKPITPETAEKLARDLKAVKYVECSALTQKGLKNVFDEAILAALE

Sequence of entity 2 (B), FASTA

>4JS0_2 Brain-specific angiogenesis inhibitor 1-associated protein 2 (chains B)
ASKSNLVISDPIPGAKPLPVPPELAPFVGRMS

Ligands and cofactors

ID	Name	Formula	Copies
GNP	Phosphoaminophosphonic acid-guanylate ester	C10 H17 N6 O13 P3	1
PE4	2-{2-[2-(2-{2-[2-(2-ethoxy-ethoxy)-ethoxy]-ethoxy}-ethoxy)-ethoxy]-ethoxy}-etha…	C16 H34 O8	3
MG	Magnesium ion	Mg	2

Primary citation

Mechanism of IRSp53 inhibition and combinatorial activation by Cdc42 and downstream effectors. Kast, D.J., Yang, C., Disanza, A. et al. Nat Struct Mol Biol (2014) 21:413-422. DOI 10.1038/nsmb.2781 · PubMed

Other PDB entries of the same protein (UniProt P60953 (AlphaFold model), which also has an AlphaFold model), best resolution first:

2NGR 1.9 Å, Transition state complex for GTP hydrolysis by CDC42: comparisons of the high resolution…
6SUP 2.0 Å, Crystal Structure of TcdB2-TccC3-Cdc42
3VHL 2.08 Å, Crystal structure of the DHR-2 domain of DOCK8 in complex with Cdc42 (T17N mutant)
1GRN 2.1 Å, Crystal structure of the CDC42/CDC42GAP/ALF3 complex.
1NF3 2.1 Å, Structure of Cdc42 in a complex with the GTPase-binding domain of the cell polarity…
2DFK 2.15 Å, Crystal structure of the CDC42-Collybistin II complex
2WM9 2.2 Å, Structure of the complex between DOCK9 and Cdc42.
2WMO 2.2 Å, Structure of the complex between DOCK9 and Cdc42.
1GZS 2.3 Å, Crystal structure of the complex between the gef domain of the salmonella typhimurium…
1KI1 2.3 Å, Guanine Nucleotide Exchange Region of Intersectin in Complex with Cdc42
3GCG 2.3 Å, crystal structure of MAP and CDC42 complex
4ITR 2.3 Å, Crystal Structure of IbpAFic2-H3717A in complex with adenylylated Cdc42

Browse structure collections

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