2IC5: Human RAC3 grown in the presence of Gpp(NH)p

Crystal structure of human RAC3 grown in the presence of Gpp(NH)p. Determined by X-ray diffraction at 1.9 Å resolution. Released 10 Oct 2006.

Method: X-ray diffraction
Resolution: 1.9 Å
Organism: Homo sapiens
Chains: 2
Atoms: 3,102
Mol. weight: 41.28 kDa
Ligands: MG, GNP, BTB, GDP
Released: 10 Oct 2006

Explore 2IC5 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

2IC5 contains 23 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: 12 helices, 6 β-strands

Element	Residues	Length	Sheet
α-helix	1	1
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	117-119	3
α-helix	123-130	8
α-helix	136-138	3
α-helix	139-148	10
β-strand	153-156	4	1
α-helix	165-177	13

Chain B: 11 helices, 6 β-strands

Element	Residues	Length	Sheet
β-strand	2-10	9	2
α-helix	16-25	10
β-strand	39-46	8	2
β-strand	49-56	8	2
α-helix	62-64	3
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	117-119	3
α-helix	123-131	9
α-helix	136-138	3
α-helix	139-149	11
β-strand	153-156	4	2
α-helix	165-177	13

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Ras-related C3 botulinum toxin substrate 3	A, B	protein	180	Homo sapiens	P60763 (AlphaFold model)

Sequence of entity 1 (A, B), FASTA

>2IC5_1 Ras-related C3 botulinum toxin substrate 3 (chains A, B)
SMQAIKCVVVGDGAVGKTCLLISYTTNAFPGEYIPTVFDNYSANVMVDGKPVNLGLWDTA
GQEDYDRLRPLSYPQTDVFLICFSLVSPASFENVRAKWYPEVRHHCPHTPILLVGTKLDL
RDDKDTIERLRDKKLAPITYPQGLAMAREIGSVKYLECSALTQRGLKTVFDEAIRAVLGG

Ligands and cofactors

ID	Name	Formula	Copies
MG	Magnesium ion	Mg	2
GNP	Phosphoaminophosphonic acid-guanylate ester	C10 H17 N6 O13 P3	1
BTB	2-[bis-(2-hydroxy-ethyl)-amino]-2-hydroxymethyl-propane-1,3-diol	C8 H19 N O5	1
GDP	Guanosine-5'-diphosphate	C10 H15 N5 O11 P2	1

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

Primary citation

Crystal structure of human RAC3 grown in the presence of Gpp(NH)p. Yang, X., Ugochukwu, E., Elkins, J. et al. To be published.

Other PDB entries of the same protein (UniProt P60763 (AlphaFold model), which also has an AlphaFold model), best resolution first:

2QME 1.75 Å, Crystal structure of human RAC3 in complex with CRIB domain of human p21-activated…
2C2H 1.85 Å, Crystal structure of the human RAC3 in complex with GDP
2G0N 1.9 Å, The Crystal Structure of the Human RAC3 in complex with GDP and Chloride
2OV2 2.1 Å, The crystal structure of the human RAC3 in complex with the CRIB domain of human…
6TM1 3.71 Å, Crystal structure of the DHR2 domain of DOCK10 in complex with RAC3

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