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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
A0006096biological_processglycolytic process
A0008361biological_processregulation of cell size
A0008865molecular_functionfructokinase activity
A0019158molecular_functionmannokinase activity
A0019318biological_processhexose metabolic process
A0031966cellular_componentmitochondrial membrane
A0046015biological_processregulation of transcription by glucose
A0051156biological_processglucose 6-phosphate metabolic process
A0098708biological_processD-glucose import across plasma membrane
A1990539biological_processfructose import across plasma membrane
A2001234biological_processnegative regulation of apoptotic signaling pathway
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues5
DetailsBinding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues1
DetailsBinding site: {"evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idMCSA1
Number of Residues
DetailsM-CSA 651
ChainResidueDetails

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PDB entries from 2026-03-25

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