1GZS: GTP-binding protein

Crystal structure of the complex between the gef domain of the salmonella typhimurium sope toxin and human Cdc42. Determined by X-ray diffraction at 2.3 Å resolution. Released 12 Sept 2002.

Method: X-ray diffraction
Resolution: 2.3 Å
Organisms: HOMO SAPIENS, SALMONELLA TYPHIMURIUM
Chains: 4
Atoms: 5,498
Mol. weight: 76.53 kDa
Released: 12 Sept 2002

Explore 1GZS in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

1GZS contains 40 α-helices and 16 β-strands across 4 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: 10 helices, 6 β-strands

Element	Residues	Length	Sheet
β-strand	2-10	9	1
α-helix	16-25	10
β-strand	41-46	6	1
β-strand	49-56	8	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	117-119	3
α-helix	123-130	8
α-helix	136-138	3
α-helix	139-148	10
β-strand	154-156	3	1
α-helix	165-177	13

Chain B: 10 helices, 2 β-strands

Element	Residues	Length	Sheet
α-helix	80-94	15
α-helix	96-102	7
α-helix	104-132	29
α-helix	138-150	13
β-strand	155-158	4	2
β-strand	161-164	4	2
α-helix	173-183	11
α-helix	185-188	4
α-helix	191-209	19
α-helix	210-213	4
α-helix	219-220	2
α-helix	221-236	16

Chain C: 10 helices, 6 β-strands

Element	Residues	Length	Sheet
β-strand	2-9	8	3
α-helix	16-25	10
β-strand	41-46	6	3
β-strand	49-56	8	3
α-helix	68-71	4
β-strand	77-83	7	3
α-helix	87-92	6
α-helix	93-97	5
α-helix	98-104	7
β-strand	110-115	6	3
α-helix	117-119	3
α-helix	123-130	8
α-helix	136-138	3
α-helix	139-148	10
β-strand	154-156	3	3
α-helix	165-176	12

Chain D: 10 helices, 2 β-strands

Element	Residues	Length	Sheet
α-helix	80-94	15
α-helix	96-102	7
α-helix	104-133	30
α-helix	138-150	13
β-strand	155-158	4	4
β-strand	161-164	4	4
α-helix	173-183	11
α-helix	185-188	4
α-helix	191-209	19
α-helix	210-213	4
α-helix	219-220	2
α-helix	221-236	16

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
GTP-binding protein	A, C	protein	180	HOMO SAPIENS	P60953 (AlphaFold model)
Sope	B, D	protein	165	SALMONELLA TYPHIMURIUM	O52623 (AlphaFold model)

Sequence of entity 1 (A, C), FASTA

>1GZS_1 GTP-BINDING PROTEIN (chains A, C)
GSMQTIKCVVVGDGAVGKTCLLISYTTNKFPSEYVPTVFDNYAVTVMIGGEPYTLGLFDT
AGQEDYDRLRPLSYPQTDVFLVCFSVVSPSSFENVKEKWVPEITHHCPKTPFLLVGTQID
LRDDPSTIEKLAKNKQKPITPETAEKLARDLKAVKYVECSALTQKGLKNVFDEAILAALE

Sequence of entity 2 (B, D), FASTA

>1GZS_2 SOPE (chains B, D)
GSLTNKVVKDFMLQTLNDIDIRGSASKDPAYASQTREAILSAVYSKNKDQCCNLLISKGI
NIAPFLQEIGEAAKNAGLPGTTKNDVFTPSGAGANPFITPLISSANSKYPRMFINQHQQA
SFKIYAEKIIMTEVAPLFNECAMPTPQQFQLILENIANKYIQNTP

Primary citation

Structural Basis for the Reversible Activation of a Rho Protein by the Bacterial Toxin Sope. Buchwald, G., Friebel, A., Galan, J.E. et al. EMBO J (2002) 21:3286. DOI 10.1093/EMBOJ/CDF329 · 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.
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

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