1GUA: Human RAP1A, residues 1-167, double mutant

Human RAP1A, residues 1-167, double mutant (E30D,K31E) complexed with gppnhp and the ras-binding-domain of human C-RAF1, residues 51-131. Determined by X-ray diffraction at 2.0 Å resolution. Released 11 Jan 1997.

Method: X-ray diffraction
Resolution: 2.0 Å
Organism: Homo sapiens
Chains: 2
Atoms: 2,062
Mol. weight: 28.83 kDa
Ligands: CA, GNP, MG
Released: 11 Jan 1997

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

Secondary structure: helices and β-sheets

1GUA 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: 8 helices, 8 β-strands

Element	Residues	Length	Sheet
β-strand	3-9	7	1
α-helix	16-25	10
β-strand	37-46	10	1
β-strand	49-57	9	1
α-helix	58-59	2
α-helix	68-74	7
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	154-165	12

Chain B: 3 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	96-102	7	1
β-strand	108-112	5	1
β-strand	117	1	3
α-helix	118-121	4
β-strand	125-130	6	1

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
RAP1A	A	protein	167	Homo sapiens	P62834 (AlphaFold model)
C-RAF1	B	protein	81	Homo sapiens	P04049 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>1GUA_1 RAP1A (chains A)
MREYKLVVLGSGGVGKSALTVQFVQGIFVDEYDPTIEDSYRKQVEVDCQQCMLEILDTAG
TEQFTAMRDLYMKNGQGFALVYSITAQSTFNDLQDLREQILRVKDTEDVPMILVGNKCDL
EDERVVGKEQGQNLARQWCNCAFLESSAKSKINVNEIFYDLVRQINR

Sequence of entity 2 (B), FASTA

>1GUA_2 C-RAF1 (chains B)
PSKTSNTIRVFLPNKQRTVVNVRNGMSLHDCLMKALKVRGLQPECCAVFRLLHEHKGKKA
RLDWNTDAASLIGEELQVDFL

Ligands and cofactors

ID	Name	Formula	Copies
CA	Calcium ion	Ca	1
GNP	Phosphoaminophosphonic acid-guanylate ester	C10 H17 N6 O13 P3	1
MG	Magnesium ion	Mg	1

Primary citation

Ras/Rap effector specificity determined by charge reversal. Nassar, N., Horn, G., Herrmann, C. et al. Nat Struct Biol (1996) 3:723-729. DOI 10.1038/nsb0896-723 · 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…
3KUC 1.92 Å, Complex of Rap1A(E30D/K31E)GDP with RafRBD(A85K/N71R)

Browse structure collections

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