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8IF6

Conformational Dynamics of the D53-D3-D14 Complex in Strigolactone Signaling

This is a non-PDB format compatible entry.
Functional Information from GO Data
ChainGOidnamespacecontents
A0005515molecular_functionprotein binding
A0005634cellular_componentnucleus
A0009414biological_processresponse to water deprivation
A0009416biological_processresponse to light stimulus
A0009926biological_processauxin polar transport
A0009934biological_processregulation of meristem structural organization
A0010016biological_processshoot system morphogenesis
A0010187biological_processnegative regulation of seed germination
A0019005cellular_componentSCF ubiquitin ligase complex
A0031146biological_processSCF-dependent proteasomal ubiquitin-dependent protein catabolic process
A0042335biological_processcuticle development
A0061137biological_processbud dilation
A1900618biological_processregulation of shoot system morphogenesis
A1902584biological_processpositive regulation of response to water deprivation
B0005515molecular_functionprotein binding
B0005634cellular_componentnucleus
B0005737cellular_componentcytoplasm
B0006511biological_processubiquitin-dependent protein catabolic process
B0009867biological_processjasmonic acid mediated signaling pathway
B0016567biological_processprotein ubiquitination
B0031146biological_processSCF-dependent proteasomal ubiquitin-dependent protein catabolic process
B0097602molecular_functioncullin family protein binding
C0005515molecular_functionprotein binding
C0005634cellular_componentnucleus
C0005737cellular_componentcytoplasm
C0010223biological_processsecondary shoot formation
C0016787molecular_functionhydrolase activity
C1901601biological_processstrigolactone biosynthetic process
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Nucleophile => ECO:0000269|PubMed:24336200
ChainResidueDetails
CSER147

site_idSWS_FT_FI2
Number of Residues2
DetailsACT_SITE: ACT_SITE => ECO:0000269|PubMed:24336200
ChainResidueDetails
CASP268
CHIS297

site_idSWS_FT_FI3
Number of Residues3
DetailsBINDING: BINDING => ECO:0000269|PubMed:26470846
ChainResidueDetails
CSER147
CCYS241
CHIS297

222926

PDB entries from 2024-07-24

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