Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

5XPS

Crystal Structure of Transketolase in complex with erythrose-4-phosphate 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 Residues4
Detailsbinding site for residue PEG A 701
ChainResidue
AASN310
APHE313
AGLN328
AASP332

site_idAC2
Number of Residues5
Detailsbinding site for residue PEG A 702
ChainResidue
ATHR198
ALYS206
ASER207
AHOH1509
AHOH1526

site_idAC3
Number of Residues6
Detailsbinding site for residue PEG A 703
ChainResidue
ALYS206
AHIS211
AILE212
AGLU214
AHOH811
AHOH821

site_idAC4
Number of Residues4
Detailsbinding site for residue PEG A 704
ChainResidue
AALA134
AASN138
ALYS139
AHOH830

site_idAC5
Number of Residues23
Detailsbinding site for residue TPP A 705
ChainResidue
AHIS66
AGLY114
ALEU116
AASP155
AGLY156
AGLU160
AASN185
AILE187
ASER188
AILE189
AILE248
AHIS261
AASP379
AGLU415
APHE442
ATYR445
AHIS478
AE4P706
ACA707
AHOH874
AHOH1046
AHOH1117
AHOH1140

site_idAC6
Number of Residues14
Detailsbinding site for residue E4P A 706
ChainResidue
AHIS27
AHIS261
AGLY262
ASER383
APHE439
AHIS466
AASP474
AARG525
ATPP705
AHOH828
AHOH840
AHOH1059
AHOH1152
AHOH1378

site_idAC7
Number of Residues5
Detailsbinding site for residue CA A 707
ChainResidue
AASP155
AASN185
AILE187
ATPP705
AHOH874

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
AHIS66
AGLY114
AASP155
AGLY156
AASN185
AILE187
AHIS261
AARG356

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

227111

PDB entries from 2024-11-06

PDB statisticsPDBj update infoContact PDBjnumon