Structure of PDB 1shz Chain A

Receptor sequence
>1shzA (length=326) Species: 10090,10116 [Search protein sequence]
AREVKLLLLGAGESGKSTFLKQMRIIHGQDFDQRAREEFRPTIYSNVIKG
MRVLVDAREKLHIPWGDNKNQLHGDKLMAFDTRAPMAAQGMVETRVFLQY
LPAIRALWEDSGIQNAYDRRREFQLGESVKYFLDNLDKLGVPDYIPSQQD
ILLARRPTKGIHETHFTFKDLHFKMFDVGGQRSERKKWFECFEGVTAIIF
CVALSDYDQVLMEDRQTNRMHESMKLFDSICNNKWFTDTSIILFLNKKDL
FEEKIKKSPLTICYPEYAGSNTYEEAAAYIQCQFEDLNKRKDTKEIYTHF
TCATDTKNVQFVFDAVTDVIIKNNLK
3D structure
PDB1shz Structure of the p115RhoGEF rgRGS domain-Galpha13/i1 chimera complex suggests convergent evolution of a GTPase activator.
ChainA
Resolution2.85 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) E58 T63 R200 D222 Q226
Catalytic site (residue number reindexed from 1) E13 T18 R155 D177 Q181
Enzyme Commision number ?
Interaction with ligand
Site
#		 Ligand Ligand
chain		 Binding residues on receptor
(original residue number in PDB)		 Binding residues on receptor
(residue number reindexed from 1)		 Binding affinity
BS01 MG A S62 T203 S17 T158
BS02 ALF A G57 E58 K61 R200 T203 G225 G12 E13 K16 R155 T158 G180
BS03 GDP A E58 S59 G60 K61 S62 T63 L197 L198 R200 N291 K292 D294 L295 T349 E13 S14 G15 K16 S17 T18 L152 L153 R155 N246 K247 D249 L250 T304
Gene Ontology
Molecular Function
GO:0003924 GTPase activity
GO:0005525 GTP binding
GO:0019001 guanyl nucleotide binding
GO:0031683 G-protein beta/gamma-subunit complex binding
Biological Process
GO:0007165 signal transduction
GO:0007186 G protein-coupled receptor signaling pathway
GO:0007188 adenylate cyclase-modulating G protein-coupled receptor signaling pathway

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Molecular Function
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Biological Process
External links
PDB RCSB:1shz, PDBe:1shz, PDBj:1shz
PDBsum1shz
PubMed15665872
UniProtP10824|GNAI1_RAT Guanine nucleotide-binding protein G(i) subunit alpha-1 (Gene Name=Gnai1);
P27601|GNA13_MOUSE Guanine nucleotide-binding protein subunit alpha-13 (Gene Name=Gna13)

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