5p21

Ligands:

,

Structural annotation:
Resources:	CATH : 5P21000 InterPro : Ipr005225, Ipr013753, Ipr001806, Ipr003577, Ipr015592 Pfam : PF00071 SCOP : d5p21__ UniProt : P01112

Functional annotation:
Cellular component:	cytoplasm membrane plasma membrane Golgi apparatus intracellular
Biological process:	small GTPase mediated signal transduction cell surface receptor linked signal transduction chemotaxis signal transduction organ morphogenesis
Molecular function:	protein binding nucleotide binding protein C-terminus binding GTP binding

Evolutionary conservation:

Toggle Conservation Colors:	Rows = identical sequences:
Further Information:	Caveats, Explanation, Complete Results at ConSurfDB

Resources:

FirstGlance, OCA, RCSB, PDBsum

Coordinates:

save as pdb, mmCIF, xml

REFINED CRYSTAL STRUCTURE OF THE TRIPHOSPHATE CONFORMATION OF H-RAS P21 AT 1.35 ANGSTROMS RESOLUTION: IMPLICATIONS FOR THE MECHANISM OF GTP HYDROLYSISREFINED CRYSTAL STRUCTURE OF THE TRIPHOSPHATE CONFORMATION OF H-RAS P21 AT 1.35 ANGSTROMS RESOLUTION: IMPLICATIONS FOR THE MECHANISM OF GTP HYDROLYSIS

Template:ABSTRACT PUBMED 2196171

About this StructureAbout this Structure

5p21 is a 1 chain structure of HRAS p21 with sequence from Homo sapiens. The April 2012 RCSB PDB Molecule of the Month feature on Ras Protein by David Goodsell is 10.2210/rcsb_pdb/mom_2012_4. Full crystallographic information is available from OCA.

ReferenceReference

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↑ Pai EF, Krengel U, Petsko GA, Goody RS, Kabsch W, Wittinghofer A. Refined crystal structure of the triphosphate conformation of H-ras p21 at 1.35 A resolution: implications for the mechanism of GTP hydrolysis. EMBO J. 1990 Aug;9(8):2351-9. PMID:2196171
↑ Ho YS, Swenson L, Derewenda U, Serre L, Wei Y, Dauter Z, Hattori M, Adachi T, Aoki J, Arai H, Inoue K, Derewenda ZS. Brain acetylhydrolase that inactivates platelet-activating factor is a G-protein-like trimer. Nature. 1997 Jan 2;385(6611):89-93. PMID:8985254 doi:10.1038/385089a0
↑ Ma J, Karplus M. Ligand-induced conformational changes in ras p21: a normal mode and energy minimization analysis. J Mol Biol. 1997 Nov 21;274(1):114-31. PMID:9398520 doi:10.1006/jmbi.1997.1313
↑ Thomas A, Bouffioux O, Geeurickx D, Brasseur R. Pex, analytical tools for PDB files. I. GF-Pex: basic file to describe a protein. Proteins. 2001 Apr 1;43(1):28-36. PMID:11170211
↑ Hayward S. Peptide-plane flipping in proteins. Protein Sci. 2001 Nov;10(11):2219-27. PMID:11604529 doi:10.1110/ps.23101
↑ Shortle D. Composites of local structure propensities: evidence for local encoding of long-range structure. Protein Sci. 2002 Jan;11(1):18-26. PMID:11742118
↑ Ermolenko DN, Thomas ST, Aurora R, Gronenborn AM, Makhatadze GI. Hydrophobic interactions at the Ccap position of the C-capping motif of alpha-helices. J Mol Biol. 2002 Sep 6;322(1):123-35. PMID:12215419
↑ Carta C, Pantaleoni F, Bocchinfuso G, Stella L, Vasta I, Sarkozy A, Digilio C, Palleschi A, Pizzuti A, Grammatico P, Zampino G, Dallapiccola B, Gelb BD, Tartaglia M. Germline missense mutations affecting KRAS Isoform B are associated with a severe Noonan syndrome phenotype. Am J Hum Genet. 2006 Jul;79(1):129-35. Epub 2006 May 1. PMID:16773572 doi:10.1086/504394

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OCA

[1] Pai EF, Krengel U, Petsko GA, Goody RS, Kabsch W, Wittinghofer A. Refined crystal structure of the triphosphate conformation of H-ras p21 at 1.35 A resolution: implications for the mechanism of GTP hydrolysis. EMBO J. 1990 Aug;9(8):2351-9. PMID:2196171

[2] Ho YS, Swenson L, Derewenda U, Serre L, Wei Y, Dauter Z, Hattori M, Adachi T, Aoki J, Arai H, Inoue K, Derewenda ZS. Brain acetylhydrolase that inactivates platelet-activating factor is a G-protein-like trimer. Nature. 1997 Jan 2;385(6611):89-93. PMID:8985254 doi:10.1038/385089a0

[3] Ma J, Karplus M. Ligand-induced conformational changes in ras p21: a normal mode and energy minimization analysis. J Mol Biol. 1997 Nov 21;274(1):114-31. PMID:9398520 doi:10.1006/jmbi.1997.1313

[4] Thomas A, Bouffioux O, Geeurickx D, Brasseur R. Pex, analytical tools for PDB files. I. GF-Pex: basic file to describe a protein. Proteins. 2001 Apr 1;43(1):28-36. PMID:11170211

[5] Hayward S. Peptide-plane flipping in proteins. Protein Sci. 2001 Nov;10(11):2219-27. PMID:11604529 doi:10.1110/ps.23101

[6] Shortle D. Composites of local structure propensities: evidence for local encoding of long-range structure. Protein Sci. 2002 Jan;11(1):18-26. PMID:11742118

[7] Ermolenko DN, Thomas ST, Aurora R, Gronenborn AM, Makhatadze GI. Hydrophobic interactions at the Ccap position of the C-capping motif of alpha-helices. J Mol Biol. 2002 Sep 6;322(1):123-35. PMID:12215419

[8] Carta C, Pantaleoni F, Bocchinfuso G, Stella L, Vasta I, Sarkozy A, Digilio C, Palleschi A, Pizzuti A, Grammatico P, Zampino G, Dallapiccola B, Gelb BD, Tartaglia M. Germline missense mutations affecting KRAS Isoform B are associated with a severe Noonan syndrome phenotype. Am J Hum Genet. 2006 Jul;79(1):129-35. Epub 2006 May 1. PMID:16773572 doi:10.1086/504394

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5p21

Contents

REFINED CRYSTAL STRUCTURE OF THE TRIPHOSPHATE CONFORMATION OF H-RAS P21 AT 1.35 ANGSTROMS RESOLUTION: IMPLICATIONS FOR THE MECHANISM OF GTP HYDROLYSISREFINED CRYSTAL STRUCTURE OF THE TRIPHOSPHATE CONFORMATION OF H-RAS P21 AT 1.35 ANGSTROMS RESOLUTION: IMPLICATIONS FOR THE MECHANISM OF GTP HYDROLYSIS

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5p21

About this StructureAbout this Structure

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ReferenceReference

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