2NGR: Protein)

Transition state complex for GTP hydrolysis by CDC42: comparisons of the high resolution structures for CDC42 bound to the active and catalytically compromised forms of the CDC42-gap. Determined by X-ray diffraction at 1.9 Å resolution. Released 6 Jan 1999.

Method: X-ray diffraction
Resolution: 1.9 Å
Organism: Homo sapiens
Chains: 2
Atoms: 3,205
Mol. weight: 48.29 kDa
Ligands: MG, GDP, AF3
Released: 6 Jan 1999

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

Secondary structure: helices and β-sheets

2NGR contains 26 α-helices and 6 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: 12 helices, 6 β-strands

Element	Residues	Length	Sheet
β-strand	2-10	9	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	117-121	5
α-helix	123-130	8
α-helix	136-138	3
α-helix	139-148	10
β-strand	154-156	3	1
α-helix	165-176	12
α-helix	179-180	2

Chain B: 14 helices, 0 β-strands

Element	Residues	Length
α-helix	269-274	6
α-helix	284-296	13
α-helix	310-321	12
α-helix	335-346	12
α-helix	355-357	3
α-helix	358-362	5
α-helix	364-366	3
α-helix	369-371	3
α-helix	372-380	9
α-helix	385-403	19
α-helix	405-408	4
α-helix	412-423	12
α-helix	429-448	20
α-helix	450-453	4

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Protein (GTP binding protein (G25K))	A	protein	191	Homo sapiens	P60953 (AlphaFold model)
Protein (gtpase activating protein (rhg))	B	protein	234	Homo sapiens	Q07960 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>2NGR_1 PROTEIN (GTP BINDING PROTEIN (G25K)) (chains A)
MQTIKCVVVGDGAVGKTCLLISYTTNKFPSEYVPTVFDNYAVTVMIGGEPYTLGLFDTAG
QEDYDRLRPLSYPQTDVFLVCFSVVSPSSFENVKEKWVPEITHHCPKTPFLLVGTQIDLR
DDPSTIEKLAKNKQKPITPETAEKLARDLKAVKYVECSALTQKGLKNVFDEAILAALEPP
EPKKSRRCVLL

Sequence of entity 2 (B), FASTA

>2NGR_2 PROTEIN (GTPASE ACTIVATING PROTEIN (RHG)) (chains B)
IPRQVLKYDDFLKSTQKSPATAPKPMPPRPPLPNQQFGVSLQHLQEKNPEQEPIPIVLRE
TVAYLQAHALTTEGIFARSANTQVVREVQQKYNMGLPVDFDQYNELHLPAVILKTFLREL
PEPLLTFDLYPHVVGFLNIDESQRVPATLQVLQTLPEENYQVLRFLTAFLVQISAHSDQN
KMTNTNLAVVFGPNLLWAKDAAITLKAINPINTFTKFLLDHQGELFPSPDPSGL

Ligands and cofactors

ID	Name	Formula	Copies
MG	Magnesium ion	Mg	1
GDP	Guanosine-5'-diphosphate	C10 H15 N5 O11 P2	1
AF3	Aluminum fluoride	Al F3	1

Primary citation

Structures of Cdc42 bound to the active and catalytically compromised forms of Cdc42GAP. Nassar, N., Hoffman, G.R., Manor, D. et al. Nat Struct Biol (1998) 5:1047-1052. DOI 10.1038/4156 · PubMed

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

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
4ITR 2.3 Å, Crystal Structure of IbpAFic2-H3717A in complex with adenylylated Cdc42

Browse structure collections

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