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1TYY

Crystal structure of aminoimidazole riboside kinase from Salmonella enterica

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0005524molecular_functionATP binding
A0006000biological_processfructose metabolic process
A0008865molecular_functionfructokinase activity
A0016301molecular_functionkinase activity
A0016740molecular_functiontransferase activity
A0046835biological_processcarbohydrate phosphorylation
A0046872molecular_functionmetal ion binding
B0000166molecular_functionnucleotide binding
B0005524molecular_functionATP binding
B0006000biological_processfructose metabolic process
B0008865molecular_functionfructokinase activity
B0016301molecular_functionkinase activity
B0016740molecular_functiontransferase activity
B0046835biological_processcarbohydrate phosphorylation
B0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE K A 404
ChainResidue
AASP246
ATHR248
AALA287
AGLY292

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE K A 405
ChainResidue
AALA180
AALA181
AALA183
AGLY213

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE K B 504
ChainResidue
BALA181
BALA183
BGLY213
BALA180

site_idAC4
Number of Residues3
DetailsBINDING SITE FOR RESIDUE K B 505
ChainResidue
BASP246
BTHR248
BALA287

Functional Information from PROSITE/UniProt
site_idPS00584
Number of Residues14
DetailsPFKB_KINASES_2 pfkB family of carbohydrate kinases signature 2. DTtGAGDafvGGLL
ChainResidueDetails
AASP246-LEU259

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsActive site: {"description":"Proton acceptor","evidences":[{"source":"PubMed","id":"15458630","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"1TZ3","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues12
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"15458630","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1TZ3","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1TZ6","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues2
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"15458630","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1TZ6","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues20
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"15458630","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"1TZ6","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues14
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"15458630","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1TYY","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1TZ3","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1TZ6","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idCSA1
Number of Residues1
DetailsAnnotated By Reference To The Literature 1lio
ChainResidueDetails
AASP252

site_idCSA2
Number of Residues1
DetailsAnnotated By Reference To The Literature 1lio
ChainResidueDetails
BASP252

site_idCSA3
Number of Residues4
DetailsAnnotated By Reference To The Literature 1lio
ChainResidueDetails
AGLY249
AGLY251
AASP252
AALA250

site_idCSA4
Number of Residues4
DetailsAnnotated By Reference To The Literature 1lio
ChainResidueDetails
BGLY249
BGLY251
BASP252
BALA250

site_idMCSA1
Number of Residues4
DetailsM-CSA 751
ChainResidueDetails
AGLY257electrostatic stabiliser
ALEU258electrostatic stabiliser
ALEU259electrostatic stabiliser
APHE260electrostatic stabiliser, proton shuttle (general acid/base)

site_idMCSA2
Number of Residues4
DetailsM-CSA 751
ChainResidueDetails
BGLY257electrostatic stabiliser
BLEU258electrostatic stabiliser
BLEU259electrostatic stabiliser
BPHE260electrostatic stabiliser, proton shuttle (general acid/base)

246031

PDB entries from 2025-12-10

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