3KUC: Ras-related protein Rap-1A

Complex of Rap1A(E30D/K31E)GDP with RafRBD(A85K/N71R). Determined by X-ray diffraction at 1.92 Å resolution. Released 23 Mar 2010.

Method: X-ray diffraction
Resolution: 1.92 Å
Organism: Homo sapiens
Chains: 2
Atoms: 2,199
Mol. weight: 28.85 kDa
Ligands: GDP, MG, CA
Released: 23 Mar 2010

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

Secondary structure: helices and β-sheets

3KUC contains 11 α-helices and 15 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: 7 helices, 8 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	62-74	13
β-strand	77-83	7	1
α-helix	87-91	5
α-helix	93-104	12
β-strand	111-116	6	1
α-helix	121-123	3
α-helix	128-137	10
β-strand	142-145	4	1
β-strand	147	1	2
β-strand	152	1	2
α-helix	154-166	13

Chain B: 4 helices, 7 β-strands

Element	Residues	Length	Sheet
β-strand	57-62	6	1
β-strand	66-71	6	1
β-strand	77	1	3
α-helix	78-87	10
α-helix	93-95	3
β-strand	96-101	6	1
α-helix	103-105	3
β-strand	109-112	4	1
β-strand	117	1	3
α-helix	119-121	3
β-strand	125-130	6	1

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Ras-related protein Rap-1A	A	protein	167	Homo sapiens	P62834 (AlphaFold model)
RAF proto-oncogene serine/threonine-protein kinase	B	protein	81	Homo sapiens	P04049 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>3KUC_1 Ras-related protein Rap-1A (chains A)
MREYKLVVLGSGGVGKSALTVQFVQGIFVDEYDPTIEDSYRKQVEVDCQQCMLEILDTAG
TEQFTAMRDLYMKNGQGFALVYSITAQSTFNDLQDLREQILRVKDTEDVPMILVGNKCDL
EDERVVGKEQGQNLARQWCNCAFLESSAKSKINVNEIFYDLVRQINR

Sequence of entity 2 (B), FASTA

>3KUC_2 RAF proto-oncogene serine/threonine-protein kinase (chains B)
PSKTSNTIRVFLPNKQRTVVRVRNGMSLHDCLMKKLKVRGLQPECCAVFRLLHEHKGKKA
RLDWNTDAASLIGEELQVDFL

Ligands and cofactors

ID	Name	Formula	Copies
GDP	Guanosine-5'-diphosphate	C10 H15 N5 O11 P2	1
MG	Magnesium ion	Mg	1
CA	Calcium ion	Ca	1

Primary citation

What makes Ras an efficient molecular switch: a computational, biophysical, and structural study of Ras-GDP interactions with mutants of Raf. Filchtinski, D., Sharabi, O., Ruppel, A. et al. J Mol Biol (2010) 399:422-435. DOI 10.1016/j.jmb.2010.03.046 · PubMed

Other PDB entries of the same protein (UniProt P62834 (AlphaFold model), which also has an AlphaFold model), best resolution first:

4KVG 1.65 Å, Crystal structure of RIAM RA-PH domains in complex with GTP bound Rap1
1C1Y 1.9 Å, Crystal structure of rap.gmppnp in complex with the ras-binding-domain of C-RAF1 kinase…
1GUA 2.0 Å, Human RAP1A, residues 1-167, double mutant (E30D,K31E) complexed with gppnhp and the…

Browse structure collections

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