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2N46

EC-NMR Structure of Human H-RasT35S mutant protein Determined by Combining Evolutionary Couplings (EC) and Sparse NMR Data

Functional Information from GO Data
ChainGOidnamespacecontents
A0003924molecular_functionGTPase activity
A0005525molecular_functionGTP binding
A0007165biological_processsignal transduction
A0016020cellular_componentmembrane
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues5
DetailsBINDING: BINDING => ECO:0000269|PubMed:16698776
ChainResidueDetails
AGLY13
AVAL29
AALA59
AASN116
ASER145

site_idSWS_FT_FI2
Number of Residues1
DetailsMOD_RES: N-acetylmethionine; in GTPase HRas; alternate => ECO:0000269|Ref.12
ChainResidueDetails
AMET1

site_idSWS_FT_FI3
Number of Residues1
DetailsMOD_RES: N-acetylthreonine; in GTPase HRas, N-terminally processed => ECO:0000269|Ref.12
ChainResidueDetails
ATHR2

site_idSWS_FT_FI4
Number of Residues1
DetailsMOD_RES: S-nitrosocysteine => ECO:0000269|PubMed:9020151
ChainResidueDetails
ACYS118

site_idSWS_FT_FI5
Number of Residues1
DetailsCARBOHYD: (Microbial infection) O-linked (Glc) threonine; by P.sordellii toxin TcsL => ECO:0000269|PubMed:19744486, ECO:0000269|PubMed:8626575, ECO:0000269|PubMed:8626586, ECO:0000269|PubMed:9632667
ChainResidueDetails
ASER35

226707

PDB entries from 2024-10-30

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