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2YHX

SEQUENCING A PROTEIN BY X-RAY CRYSTALLOGRAPHY. II. REFINEMENT OF YEAST HEXOKINASE B CO-ORDINATES AND SEQUENCE AT 2.1 ANGSTROMS RESOLUTION

Replaces:  1YHX
Functional Information from GO Data
ChainGOidnamespacecontents
A0001678biological_processintracellular glucose homeostasis
A0004340molecular_functionglucokinase activity
A0004396molecular_functionhexokinase activity
A0005515molecular_functionprotein binding
A0005524molecular_functionATP binding
A0005536molecular_functionD-glucose binding
A0005634cellular_componentnucleus
A0005739cellular_componentmitochondrion
A0005829cellular_componentcytosol
A0005975biological_processcarbohydrate metabolic process
A0006000biological_processfructose metabolic process
A0006006biological_processglucose metabolic process
A0006013biological_processmannose metabolic process
A0006091biological_processgeneration of precursor metabolites and energy
A0006096biological_processglycolytic process
A0008361biological_processregulation of cell size
A0008865molecular_functionfructokinase activity
A0016301molecular_functionkinase activity
A0016773molecular_functionphosphotransferase activity, alcohol group as acceptor
A0019158molecular_functionmannokinase activity
A0019318biological_processhexose metabolic process
A0019637biological_processorganophosphate metabolic process
A0031966cellular_componentmitochondrial membrane
A0046015biological_processregulation of transcription by glucose
A0046323biological_processglucose import
A0046835biological_processcarbohydrate phosphorylation
A0051156biological_processglucose 6-phosphate metabolic process
A1901135biological_processcarbohydrate derivative metabolic process
A1990539biological_processfructose import across plasma membrane
A2001234biological_processnegative regulation of apoptotic signaling pathway
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues10
DetailsBINDING: BINDING => ECO:0000250
ChainResidueDetails
AMET69
AUNK402
AGLY141
APHE158
AILE193
ACYS220
AALA252
AUNK285
AARG290
ALEU327

site_idSWS_FT_FI2
Number of Residues1
DetailsBINDING: BINDING => ECO:0000255
ChainResidueDetails
ASER94

site_idSWS_FT_FI3
Number of Residues1
DetailsMOD_RES: Phosphothreonine => ECO:0007744|PubMed:18407956
ChainResidueDetails
APRO21

site_idSWS_FT_FI4
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0000269|PubMed:9047292, ECO:0007744|PubMed:18407956
ChainResidueDetails
AGLY141

site_idSWS_FT_FI5
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:19779198
ChainResidueDetails
AALA228

site_idSWS_FT_FI6
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P04806
ChainResidueDetails
ASER255

Catalytic Information from CSA
site_idMCSA1
Number of Residues3
DetailsM-CSA 651
ChainResidueDetails
AGLY141electrostatic stabiliser
AUNK156electrostatic stabiliser
ALEU194proton shuttle (general acid/base)

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PDB entries from 2024-07-31

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