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5I5E

Crystal Structure of Transketolase mutants-H66/261C complex with xylulose-5-phoaphate from Pichia Stipitis

Functional Information from GO Data
ChainGOidnamespacecontents
A0003824molecular_functioncatalytic activity
A0004802molecular_functiontransketolase activity
A0005634cellular_componentnucleus
A0005829cellular_componentcytosol
A0006098biological_processpentose-phosphate shunt
A0016740molecular_functiontransferase activity
A0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues25
Detailsbinding site for residue TPP A 701
ChainResidue
AALA30
AILE187
ASER188
AILE189
AILE248
ACYS261
AASP379
AGLU415
APHE442
ATYR445
AHIS478
ACYS66
A5SP702
ACA703
AHOH843
AHOH998
AHOH1043
AHOH1234
AGLY114
APRO115
ALEU116
AASP155
AGLY156
AGLU160
AASN185

site_idAC2
Number of Residues14
Detailsbinding site for residue 5SP A 702
ChainResidue
AHIS27
ACYS66
AHIS100
AILE189
AARG356
ASER383
APHE439
AHIS466
AASP474
AHIS478
AARG525
ATPP701
AHOH801
AHOH1142

site_idAC3
Number of Residues5
Detailsbinding site for residue CA A 703
ChainResidue
AASP155
AASN185
AILE187
ATPP701
AHOH998

Functional Information from PROSITE/UniProt
site_idPS00801
Number of Residues21
DetailsTRANSKETOLASE_1 Transketolase signature 1. RllaVDavaaanSGHPGapLG
ChainResidueDetails
AARG13-GLY33

site_idPS00802
Number of Residues17
DetailsTRANSKETOLASE_2 Transketolase signature 2. GEDGPTHqPIEtlAhfR
ChainResidueDetails
AGLY472-ARG488

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Proton donor => ECO:0000250
ChainResidueDetails
AGLU415

site_idSWS_FT_FI2
Number of Residues15
DetailsBINDING: BINDING => ECO:0000250
ChainResidueDetails
AHIS27
ASER383
AGLU415
APHE442
AHIS466
AASP474
AARG525
ACYS66
AGLY114
AASP155
AGLY156
AASN185
AILE187
ACYS261
AARG356

site_idSWS_FT_FI3
Number of Residues2
DetailsSITE: Important for catalytic activity => ECO:0000250
ChainResidueDetails
AHIS27
ACYS261

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PDB entries from 2024-11-06

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