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6XXG

Structure of truncated 1-deoxy-D-xylulose 5-phosphate synthase (DXS) from Deinococcus radiodurans

This is a non-PDB format compatible entry.
Functional Information from GO Data
ChainGOidnamespacecontents
AAA0003824molecular_functioncatalytic activity
AAA0008661molecular_function1-deoxy-D-xylulose-5-phosphate synthase activity
AAA0016114biological_processterpenoid biosynthetic process
BBB0003824molecular_functioncatalytic activity
BBB0008661molecular_function1-deoxy-D-xylulose-5-phosphate synthase activity
BBB0016114biological_processterpenoid biosynthetic process
Functional Information from PROSITE/UniProt
site_idPS00802
Number of Residues17
DetailsTRANSKETOLASE_2 Transketolase signature 2. GADGATHnGVFdlSflR
ChainResidueDetails
AAAGLY428-ARG444

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues8
DetailsBINDING: BINDING => ECO:0000269|PubMed:17135236
ChainResidueDetails
AAAHIS82
AAAASP154
AAAASN183
AAAGLU373
BBBHIS82
BBBASP154
BBBASN183
BBBGLU373

site_idSWS_FT_FI2
Number of Residues4
DetailsBINDING:
ChainResidueDetails
AAAGLY123
AAAGLY155
BBBGLY123
BBBGLY155

Catalytic Information from CSA
site_idMCSA1
Number of Residues3
DetailsM-CSA 333
ChainResidueDetails
AAALYS289electrostatic stabiliser
AAAGLU373activator, electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
AAAARG401electrostatic stabiliser, hydrogen bond donor

site_idMCSA2
Number of Residues3
DetailsM-CSA 333
ChainResidueDetails
BBBLYS289electrostatic stabiliser
BBBGLU373activator, electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
BBBARG401electrostatic stabiliser, hydrogen bond donor

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PDB entries from 2024-09-04

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