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5I5G

Crystal Structure of Transketolase mutant-R525L from Pichia Stipitis

Functional Information from GO Data
ChainGOidnamespacecontents
A0003824molecular_functioncatalytic activity
A0004802molecular_functiontransketolase activity
A0005634cellular_componentnucleus
A0005829cellular_componentcytosol
A0006098biological_processpentose-phosphate shunt
A0006163biological_processpurine nucleotide metabolic process
A0016740molecular_functiontransferase activity
A0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues12
Detailsbinding site for residue POP A 701
ChainResidue
AALA30
AHOH801
AHOH814
AHOH920
AHIS66
AGLY154
AASP155
AGLY156
AASN185
AILE187
AILE248
AHIS261

site_idAC2
Number of Residues4
Detailsbinding site for residue PEG A 702
ChainResidue
AALA427
AGLU457
ATHR515
AHOH816

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
AHIS66
AGLY114
AASP155
AGLY156
AASN185
AILE187
AHIS261
AARG356
ASER383
AGLU415
APHE442
AHIS466
AASP474
ALEU525
AHIS27

site_idSWS_FT_FI3
Number of Residues2
DetailsSITE: Important for catalytic activity => ECO:0000250
ChainResidueDetails
AHIS27
AHIS261

219869

PDB entries from 2024-05-15

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