2QRZ: Cdc42

Cdc42 bound to GMP-PCP: Induced Fit by Effector is Required. Determined by X-ray diffraction at 2.4 Å resolution. Released 18 Mar 2008.

Method: X-ray diffraction
Resolution: 2.4 Å
Organism: Homo sapiens
Chains: 2
Atoms: 3,117
Mol. weight: 43.3 kDa
Ligands: GCP, MG
Released: 18 Mar 2008

Explore 2QRZ in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

2QRZ contains 19 α-helices and 12 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	2-10	9	1
α-helix	16-25	10
β-strand	39-46	8	1
β-strand	49-56	8	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	117-121	5
α-helix	123-130	8
α-helix	136-138	3
α-helix	139-149	11
β-strand	154-156	3	1
α-helix	165-176	12

Chain B: 8 helices, 6 β-strands

Element	Residues	Length	Sheet
β-strand	2-10	9	2
α-helix	16-25	10
β-strand	40-46	7	2
β-strand	49-56	8	2
α-helix	68-71	4
β-strand	77-83	7	2
α-helix	87-92	6
α-helix	93-97	5
α-helix	98-104	7
β-strand	110-115	6	2
α-helix	124-131	8
α-helix	139-148	10
β-strand	154-156	3	2
α-helix	165-174	10

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Cell division control protein 42 homolog precursor	A, B	protein	189	Homo sapiens	P60953 (AlphaFold model)

Sequence of entity 1 (A, B), FASTA

>2QRZ_1 Cell division control protein 42 homolog precursor (chains A, B)
MQTIKCVVVGDGAVGKTCLLISYTTNKFPSEYVPTVFDNYAVTVMIGGEPYTLGLFDTAG
QEDYDRLRPLSYPQTDVFLVCFSVVSPSSFENVKEKWVPEITHHCPKTPFLLVGTQIDLR
DDPSTIEKLAKNKQKPITPETAEKLARDLKAVKYVECSALTQKGLKNVFDEAILAALEPP
EPKKSRRCV

Ligands and cofactors

ID	Name	Formula	Copies
GCP	Phosphomethylphosphonic acid guanylate ester	C11 H18 N5 O13 P3	2
MG	Magnesium ion	Mg	2

Water and common crystallization additives (SO4) are not listed.

Primary citation

Effector Proteins Exert an Important Influence on the Signaling-active State of the Small GTPase Cdc42. Phillips, M.J., Calero, G., Chan, B. et al. J Biol Chem (2008) 283:14153-14164. DOI 10.1074/jbc.M706271200 · 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…
4JS0 1.9 Å, Complex of Cdc42 with the CRIB-PR domain of IRSp53
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

Browse structure collections

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