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1EX6

CRYSTAL STRUCTURE OF UNLIGANDED FORM OF GUANYLATE KINASE FROM YEAST

Functional Information from GO Data
ChainGOidnamespacecontents
A0004385molecular_functionguanylate kinase activity
A0005524molecular_functionATP binding
A0005634cellular_componentnucleus
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0006163biological_processpurine nucleotide metabolic process
A0016301molecular_functionkinase activity
A0016310biological_processphosphorylation
A0046037biological_processGMP metabolic process
A0046711biological_processGDP biosynthetic process
B0004385molecular_functionguanylate kinase activity
B0005524molecular_functionATP binding
B0005634cellular_componentnucleus
B0005737cellular_componentcytoplasm
B0005829cellular_componentcytosol
B0006163biological_processpurine nucleotide metabolic process
B0016301molecular_functionkinase activity
B0016310biological_processphosphorylation
B0046037biological_processGMP metabolic process
B0046711biological_processGDP biosynthetic process
Functional Information from PROSITE/UniProt
site_idPS00856
Number of Residues18
DetailsGUANYLATE_KINASE_1 Guanylate kinase-like signature. TTRtpRagEvnGkdYnFV
ChainResidueDetails
ATHR36-VAL53

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00100
ChainResidueDetails
APRO9
BPRO209

site_idSWS_FT_FI2
Number of Residues12
DetailsBINDING: BINDING => ECO:0000269|PubMed:1314905, ECO:0000269|PubMed:1967656, ECO:0007744|PDB:1GKY
ChainResidueDetails
ASER35
BTRP270
BGLY279
BMET301
ATHR39
AASN51
ATRP70
AGLY79
AMET101
BSER235
BTHR239
BASN251

site_idSWS_FT_FI3
Number of Residues2
DetailsMOD_RES: N-acetylserine => ECO:0000269|PubMed:1314905, ECO:0000269|PubMed:2551688
ChainResidueDetails
AARG2
BARG202

site_idSWS_FT_FI4
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:17287358, ECO:0007744|PubMed:17330950, ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198
ChainResidueDetails
AALA149
BALA349

site_idSWS_FT_FI5
Number of Residues2
DetailsMOD_RES: Phosphotyrosine => ECO:0007744|PubMed:19779198
ChainResidueDetails
AALA157
BALA357

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PDB entries from 2024-10-09

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