Brand  (β version)

PDB ID: 1C1Y

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Ligands
Code Name Style Show Link
CA Calcium ion PoSSuM
GTP Guanosine-5'-triphosphate PoSSuM
MG Magnesium ion PoSSuM
Non-standard Residues
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Glycosylation
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Structure summary

Code : 1C1Y   PDBj   RCSB PDB   PDBe
Header : SIGNALING PROTEIN
Title : CRYSTAL STRUCTURE OF RAP.GMPPNP IN COMPLEX WITH THE RAS-BINDING-DOMAIN OF C-RAF1 KINASE (RAFRBD).
Release Data : 1999-08-02
Compound :
mol_id molecule chains
1 RAS-RELATED PROTEIN RAP-1A A
fragment: RAP, RESIDUES 1-167
mol_id molecule chains
2 PROTO-ONCOGENE SERINE/THREONINE PROTEIN KINASE RAF-1 B
ec: 2.7.1.-
fragment: RAFRBD, RESIDUES 51-131
Source :
mol_id organism_scientific organism_common expression_system
1 Homo sapiens  (taxid:9606) Human Escherichia coli  (taxid:562)
expression_system_vector_type: PLASMID
expression_system_plasmid: PBKS
mol_id organism_scientific organism_common expression_system
2 Homo sapiens  (taxid:9606) Human Escherichia coli  (taxid:562)
expression_system_vector_type: PLASMID
expression_system_plasmid: PGEX-2T
Authors : Nassar, N.
Keywords : GTP-BINDING PROTEINS, PROTEIN-PROTEIN COMPLEX, EFFECTORS, SIGNALING PROTEIN
Exp. method : X-RAY DIFFRACTION ( 1.90 Å )
Citation :

The 2.2 A crystal structure of the Ras-binding domain of the serine/threonine kinase c-Raf1 in complex with Rap1A and a GTP analogue.

Nassar, N.
(1995)  Nature  375 : 554 - 560

PubMed: 7791872
DOI: 10.1038/375554a0

Ras/Rap effector specificty determined by charge reversal.

Nassar, N.
(1996)  Nat.Struct.Biol.  3 : 723 - 729

Structure of Epac2 in complex with a cyclic AMP analogue and RAP1B.

Rehmann, H.,Arias-Palomo, E.,Hadders, M.A.  et al.
(2008)  Nature  455 : 124 - 127

PubMed: 18660803
DOI: 10.1038/nature07187

Reaction

Chain : A
UniProt : P62834 (RAP1A_HUMAN)
Reaction: EC: Evidence:
Physiological Direction:
GTP + H2O = GDP + H(+) + phosphate 3.6.5.2 UniProtKB:P61224
-
Chain : B
UniProt : P04049 (RAF1_HUMAN)
Reaction: EC: Evidence:
Physiological Direction:
ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl- [protein] 2.7.11.1 PubMed:17603483
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ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L- threonyl-[protein] 2.7.11.1 PubMed:17603483
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