2OV2: Human RAC3

The crystal structure of the human RAC3 in complex with the CRIB domain of human p21-activated kinase 4 (PAK4). Determined by X-ray diffraction at 2.1 Å resolution. Released 13 Mar 2007.

Method: X-ray diffraction
Resolution: 2.1 Å
Organism: Homo sapiens
Chains: 16
Atoms: 14,479
Mol. weight: 197.57 kDa
Ligands: MG, GCP
Released: 13 Mar 2007

Explore 2OV2 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

2OV2 contains 103 α-helices and 80 β-strands across 16 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	2-9	8	1
α-helix	16-25	10
β-strand	37-46	10	1
β-strand	49-57	9	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	123-131	9
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	3-10	8	3
α-helix	16-25	10
β-strand	37-46	10	3
β-strand	49-58	10	3
α-helix	62-64	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	153-156	4	3
α-helix	165-176	12

Chains C and G: 11 helices, 6 β-strands

Element	Residues	Length	Sheet
β-strand	2-10	9	4
α-helix	16-25	10
β-strand	37-46	10	4
β-strand	49-58	10	4
α-helix	62-64	3
α-helix	68-71	4
β-strand	77-83	7	4
α-helix	87-92	6
α-helix	93-97	5
α-helix	98-104	7
β-strand	110-115	6	4
α-helix	117-120	4
α-helix	123-131	9
α-helix	136-138	3
α-helix	139-148	10
β-strand	153-156	4	4
α-helix	165-177	13

Chain D: 11 helices, 6 β-strands

Element	Residues	Length	Sheet
β-strand	2-10	9	6
α-helix	16-25	10
β-strand	37-46	10	6
β-strand	49-58	10	6
α-helix	62-64	3
α-helix	68-71	4
β-strand	77-83	7	6
α-helix	87-92	6
α-helix	93-97	5
α-helix	98-104	7
β-strand	110-115	6	6
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	6
α-helix	165-177	13

Chain E: 11 helices, 6 β-strands

Element	Residues	Length	Sheet
β-strand	3-10	8	7
α-helix	16-25	10
β-strand	37-46	10	7
β-strand	49-58	10	7
α-helix	62-64	3
α-helix	68-71	4
β-strand	77-83	7	7
α-helix	87-92	6
α-helix	93-97	5
α-helix	98-104	7
β-strand	110-115	6	7
α-helix	117-119	3
α-helix	123-131	9
α-helix	136-138	3
α-helix	139-148	10
β-strand	153-156	4	7
α-helix	165-177	13

Chain F: 11 helices, 6 β-strands

Element	Residues	Length	Sheet
β-strand	3-10	8	2
α-helix	16-25	10
β-strand	37-46	10	2
β-strand	49-58	10	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	117-120	4
α-helix	123-131	9
α-helix	136-138	3
α-helix	139-148	10
β-strand	153-156	4	2
α-helix	165-177	13

Chain H: 11 helices, 6 β-strands

Element	Residues	Length	Sheet
β-strand	3-10	8	8
α-helix	16-25	10
β-strand	37-46	10	8
β-strand	49-58	10	8
α-helix	62-64	3
α-helix	68-71	4
β-strand	77-83	7	8
α-helix	87-92	6
α-helix	93-97	5
α-helix	98-104	7
β-strand	110-115	6	8
α-helix	117-120	4
α-helix	125-130	6
α-helix	136-138	3
α-helix	139-148	10
β-strand	153-156	4	8
α-helix	165-177	13

Chains I, M and O: 2 helices, 4 β-strands

Element	Residues	Length	Sheet
β-strand	11	1	1
α-helix	12-14	3
β-strand	15-23	9	1
β-strand	24-26	3	9
β-strand	31-33	3	9
α-helix	37-39	3

4 more chain groups are not listed. Open the entry in the viewer and use the sequence panel to see them.

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Ras-related C3 botulinum toxin substrate 3	A, B, C, D, E, F, G, H	protein	179	Homo sapiens	P60763 (AlphaFold model)
Serine/threonine-protein kinase PAK 4	I, J, K, L, M, N, O, P	protein	35	Homo sapiens	O96013 (AlphaFold model)

Sequence of entity 1 (A, B, C, D, E, F, G, H), FASTA

>2OV2_1 Ras-related C3 botulinum toxin substrate 3 (chains A, B, C, D, E, F, G, H)
SMQAIKCVVVGDGAVGKTCLLISYTTNAFPGEYIPTVFDNYSANVMVDGKPVNLGLWDTA
GQEDYDRLRPLSYPQTDVFLICFSLVSPASFENVRAKWYPEVRHHCPHTPILLVGTKLDL
RDDKDTIERLRDKKLAPITYPQGLAMAREIGSVKYLECSALTQRGLKTVFDEAIRAVLG

Sequence of entity 2 (I, J, K, L, M, N, O, P), FASTA

>2OV2_2 Serine/threonine-protein kinase PAK 4 (chains I, J, K, L, M, N, O, P)
EISAPSNFEHRVHTGFDQHEQKFTGLPRQWQSLIE

Ligands and cofactors

ID	Name	Formula	Copies
MG	Magnesium ion	Mg	8
GCP	Phosphomethylphosphonic acid guanylate ester	C11 H18 N5 O13 P3	8

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

Primary citation

The crystal structure of the human RAC3 in complex with the CRIB domain of human p21-activated kinase 4 (PAK4). Ugochukwu, E., Yang, X., Elkins, J.M. 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
2IC5 1.9 Å, Crystal structure of human RAC3 grown in the presence of Gpp(NH)p.
6TM1 3.71 Å, Crystal structure of the DHR2 domain of DOCK10 in complex with RAC3

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