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1UF9

Crystal structure of TT1252 from Thermus thermophilus

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0004140molecular_functiondephospho-CoA kinase activity
A0005524molecular_functionATP binding
A0005737cellular_componentcytoplasm
A0015937biological_processcoenzyme A biosynthetic process
A0016301molecular_functionkinase activity
A0016310biological_processphosphorylation
A0016740molecular_functiontransferase activity
B0000166molecular_functionnucleotide binding
B0004140molecular_functiondephospho-CoA kinase activity
B0005524molecular_functionATP binding
B0005737cellular_componentcytoplasm
B0015937biological_processcoenzyme A biosynthetic process
B0016301molecular_functionkinase activity
B0016310biological_processphosphorylation
B0016740molecular_functiontransferase activity
C0000166molecular_functionnucleotide binding
C0004140molecular_functiondephospho-CoA kinase activity
C0005524molecular_functionATP binding
C0005737cellular_componentcytoplasm
C0015937biological_processcoenzyme A biosynthetic process
C0016301molecular_functionkinase activity
C0016310biological_processphosphorylation
C0016740molecular_functiontransferase activity
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE PO4 B 600
ChainResidue
BGLY20
BLYS21
BSER22
BARG145

site_idAC2
Number of Residues12
DetailsBINDING SITE FOR RESIDUE ATP C 500
ChainResidue
CLYS21
CSER22
CTHR23
CARG141
CARG145
CASN176
CTHR177
CASN16
CILE17
CGLY18
CSER19
CGLY20

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues9
DetailsBINDING: BINDING => ECO:0000269|PubMed:15526298, ECO:0007744|PDB:1UF9
ChainResidueDetails
AASN16
AARG145
AASN176
BASN16
BARG145
BASN176
CASN16
CARG145
CASN176

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PDB entries from 2024-04-24

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