3GCG: MAP and CDC42 complex

crystal structure of MAP and CDC42 complex. Determined by X-ray diffraction at 2.3 Å resolution. Released 21 Jul 2009.

Method: X-ray diffraction
Resolution: 2.3 Å
Organisms: Homo sapiens, Escherichia coli
Chains: 2
Atoms: 2,767
Mol. weight: 39.78 kDa
Released: 21 Jul 2009

Explore 3GCG in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

3GCG contains 16 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: 9 helices, 6 β-strands

Element	Residues	Length	Sheet
β-strand	3-10	8	1
α-helix	16-24	9
β-strand	40-46	7	1
β-strand	49-57	9	1
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	123-127	5
α-helix	136-138	3
α-helix	139-148	10
β-strand	154-156	3	1
α-helix	165-176	12

Chain B: 7 helices, 2 β-strands

Element	Residues	Length	Sheet
α-helix	51-63	13
α-helix	72-98	27
α-helix	104-118	15
α-helix	130-136	7
α-helix	139-149	11
α-helix	155-177	23
β-strand	179	1	2
β-strand	181	1	2
α-helix	183-197	15

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Cell division control protein 42 homolog	A	protein	182	Homo sapiens	P60953 (AlphaFold model)
L0028 (Mitochondria associated protein)	B	protein	172	Escherichia coli	Q9R8E4 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>3GCG_1 Cell division control protein 42 homolog (chains A)
GPLGSQTIKCVVVGDGAVGKTCLLISYTTNKFPSEYVPTVFDNYAVTVMIGGEPYTLGLF
DTAGQEDYDRLRPLSYPQTDVFLVCFSVVSPSSFENVKEKWVPEITHHCPKTPFLLVGTQ
IDLRDDPSTIEKLAKNKQKPITPETAEKLARDLKAVKYVECSALTQKGLKNVFDEAILAA
LE

Sequence of entity 2 (B), FASTA

>3GCG_2 L0028 (Mitochondria associated protein) (chains B)
GPLGSGMRFMPVQSNFVINHGKLTNQLLQAVAKQTRNGDTQQWFQQEQTTYISRTVNRTL
DDYCRSNNSVISKETKGHIFRAVENALQQPLDMNGAQSSIGHFLQSNKYFNQKVDEQCGK
RVDPITRFNTQTKMIEQVSQEIFERNFSGFKVSEIKAITQNAILEHVQDTRL

Primary citation

Structural insights into host GTPase isoform selection by a family of bacterial GEF mimics. Huang, Z., Sutton, S.E., Wallenfang, A.J. et al. Nat Struct Mol Biol (2009) 16:853-860. DOI 10.1038/nsmb.1647 · 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
4ITR 2.3 Å, Crystal Structure of IbpAFic2-H3717A in complex with adenylylated Cdc42

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