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

5XQK

Crystal Structure of Transketolase in complex with xylulose-5-phosphate from Pichia Stipitis

Functional Information from GO Data
ChainGOidnamespacecontents
A0003824molecular_functioncatalytic activity
A0004802molecular_functiontransketolase activity
A0006163biological_processpurine nucleotide metabolic process
A0016740molecular_functiontransferase activity
A0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues37
Detailsbinding site for residue T5X A 701
ChainResidue
AHIS27
AASN185
AILE187
ASER188
AILE189
AILE248
AHIS261
AASP379
ASER383
AGLU415
APHE439
AALA30
APHE442
ATYR445
AHIS466
AASP474
AHIS478
AARG525
ACA702
AHOH820
AHOH845
AHOH911
AHIS66
AHOH955
AHOH988
AHOH997
AHOH1008
AHOH1014
AHOH1080
AHOH1117
AHOH1150
AHIS100
AGLY114
ALEU116
AASP155
AGLY156
AGLU160

site_idAC2
Number of Residues5
Detailsbinding site for residue CA A 702
ChainResidue
AASP155
AASN185
AILE187
AT5X701
AHOH911

site_idAC3
Number of Residues3
Detailsbinding site for residue PEG A 703
ChainResidue
AALA134
AASN138
AHOH808

site_idAC4
Number of Residues3
Detailsbinding site for residue PEG A 704
ChainResidue
AASN310
ALEU331
AASP332

site_idAC5
Number of Residues6
Detailsbinding site for residue PEG A 705
ChainResidue
AASN103
ATHR104
APRO107
AHOH827
AHOH917
AHOH947

site_idAC6
Number of Residues6
Detailsbinding site for residue PEG A 706
ChainResidue
AGLN526
AALA639
APRO640
APHE643
AHOH1354
AHOH1401

site_idAC7
Number of Residues5
Detailsbinding site for residue PEG A 707
ChainResidue
ALYS206
AHIS211
AILE212
AGLU214
AHOH803

site_idAC8
Number of Residues5
Detailsbinding site for residue PEG A 708
ChainResidue
ATHR198
AHOH802
AHOH871
AHOH1170
AHOH1230

site_idAC9
Number of Residues3
Detailsbinding site for residue PEG A 709
ChainResidue
AGLU85
ALYS88
ASER284

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

223166

PDB entries from 2024-07-31

PDB statisticsPDBj update infoContact PDBjnumon