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

4QS9

Arabidopsis Hexokinase 1 (AtHXK1) mutant S177A structure in glucose-bound form

Functional Information from GO Data
ChainGOidnamespacecontents
A0000325cellular_componentplant-type vacuole
A0001046molecular_functioncore promoter sequence-specific DNA binding
A0001678biological_processintracellular glucose homeostasis
A0004340molecular_functionglucokinase activity
A0004396molecular_functionhexokinase activity
A0005515molecular_functionprotein binding
A0005524molecular_functionATP binding
A0005536molecular_functionD-glucose binding
A0005634cellular_componentnucleus
A0005737cellular_componentcytoplasm
A0005739cellular_componentmitochondrion
A0005741cellular_componentmitochondrial outer membrane
A0005975biological_processcarbohydrate metabolic process
A0006096biological_processglycolytic process
A0006357biological_processregulation of transcription by RNA polymerase II
A0008270molecular_functionzinc ion binding
A0008865molecular_functionfructokinase activity
A0009750biological_processresponse to fructose
A0010148biological_processtranspiration
A0010182biological_processsugar mediated signaling pathway
A0010255biological_processglucose mediated signaling pathway
A0012501biological_processprogrammed cell death
A0016301molecular_functionkinase activity
A0016310biological_processphosphorylation
A0016773molecular_functionphosphotransferase activity, alcohol group as acceptor
A0019318biological_processhexose metabolic process
A0019320biological_processhexose catabolic process
A0032991cellular_componentprotein-containing complex
A0043231cellular_componentintracellular membrane-bounded organelle
A0046835biological_processcarbohydrate phosphorylation
A0051156biological_processglucose 6-phosphate metabolic process
A0090332biological_processstomatal closure
A2000032biological_processregulation of secondary shoot formation
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues5
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:Q8LQ68
ChainResidueDetails
AGLY104
ATHR105
AASN106
ATHR253
AGLY441

site_idSWS_FT_FI2
Number of Residues7
DetailsBINDING: BINDING => ECO:0000269|PubMed:25664748, ECO:0007744|PDB:4QS7, ECO:0007744|PDB:4QS9
ChainResidueDetails
ATHR194
ALYS195
AASN229
AASP230
AASN256
AGLU284
AGLU315

226707

PDB entries from 2024-10-30

PDB statisticsPDBj update infoContact PDBjnumon