Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

3UC4

The crystal structure of Snf1-related kinase 2.6

Functional Information from GO Data
ChainGOidnamespacecontents
A0004672molecular_functionprotein kinase activity
A0004674molecular_functionprotein serine/threonine kinase activity
A0005515molecular_functionprotein binding
A0005524molecular_functionATP binding
A0005634cellular_componentnucleus
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0005886cellular_componentplasma membrane
A0005985biological_processsucrose metabolic process
A0006468biological_processprotein phosphorylation
A0006636biological_processunsaturated fatty acid biosynthetic process
A0006952biological_processdefense response
A0006970biological_processresponse to osmotic stress
A0009414biological_processresponse to water deprivation
A0009651biological_processresponse to salt stress
A0009737biological_processresponse to abscisic acid
A0009738biological_processabscisic acid-activated signaling pathway
A0009789biological_processpositive regulation of abscisic acid-activated signaling pathway
A0009931molecular_functioncalcium-dependent protein serine/threonine kinase activity
A0010118biological_processstomatal movement
A0010119biological_processregulation of stomatal movement
A0010359biological_processregulation of anion channel activity
A0016301molecular_functionkinase activity
A0019432biological_processtriglyceride biosynthetic process
A0019903molecular_functionprotein phosphatase binding
A0042742biological_processdefense response to bacterium
A0042802molecular_functionidentical protein binding
A0046777biological_processprotein autophosphorylation
A0048366biological_processleaf development
A0071244biological_processcellular response to carbon dioxide
A0071485biological_processcellular response to absence of light
A0090333biological_processregulation of stomatal closure
A0106310molecular_functionprotein serine kinase activity
A1902456biological_processregulation of stomatal opening
A2000377biological_processregulation of reactive oxygen species metabolic process
B0004672molecular_functionprotein kinase activity
B0004674molecular_functionprotein serine/threonine kinase activity
B0005515molecular_functionprotein binding
B0005524molecular_functionATP binding
B0005634cellular_componentnucleus
B0005737cellular_componentcytoplasm
B0005829cellular_componentcytosol
B0005886cellular_componentplasma membrane
B0005985biological_processsucrose metabolic process
B0006468biological_processprotein phosphorylation
B0006636biological_processunsaturated fatty acid biosynthetic process
B0006952biological_processdefense response
B0006970biological_processresponse to osmotic stress
B0009414biological_processresponse to water deprivation
B0009651biological_processresponse to salt stress
B0009737biological_processresponse to abscisic acid
B0009738biological_processabscisic acid-activated signaling pathway
B0009789biological_processpositive regulation of abscisic acid-activated signaling pathway
B0009931molecular_functioncalcium-dependent protein serine/threonine kinase activity
B0010118biological_processstomatal movement
B0010119biological_processregulation of stomatal movement
B0010359biological_processregulation of anion channel activity
B0016301molecular_functionkinase activity
B0019432biological_processtriglyceride biosynthetic process
B0019903molecular_functionprotein phosphatase binding
B0042742biological_processdefense response to bacterium
B0042802molecular_functionidentical protein binding
B0046777biological_processprotein autophosphorylation
B0048366biological_processleaf development
B0071244biological_processcellular response to carbon dioxide
B0071485biological_processcellular response to absence of light
B0090333biological_processregulation of stomatal closure
B0106310molecular_functionprotein serine kinase activity
B1902456biological_processregulation of stomatal opening
B2000377biological_processregulation of reactive oxygen species metabolic process
Functional Information from PROSITE/UniProt
site_idPS00107
Number of Residues24
DetailsPROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. IGSGNFGVARlMrdkqsnel..........VAVK
ChainResidueDetails
AILE27-LYS50

site_idPS00108
Number of Residues13
DetailsPROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. VcHrDLKleNTLL
ChainResidueDetails
AVAL136-LEU148

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-ProRule:PRU10027
ChainResidueDetails
AASP140
BASP140

site_idSWS_FT_FI2
Number of Residues4
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00159
ChainResidueDetails
AILE27
ALYS50
BILE27
BLYS50

site_idSWS_FT_FI3
Number of Residues8
DetailsMOD_RES: Phosphoserine; by autocatalysis => ECO:0000269|PubMed:16766677
ChainResidueDetails
ASER7
ASER18
ASER29
ASER43
BSER7
BSER18
BSER29
BSER43

site_idSWS_FT_FI4
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0000269|PubMed:16766677
ChainResidueDetails
ASER175
BSER175

219140

PDB entries from 2024-05-01

PDB statisticsPDBj update infoContact PDBjnumon