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

1GPU

Transketolase complex with reaction intermediate

Functional Information from GO Data
ChainGOidnamespacecontents
A0003824molecular_functioncatalytic activity
A0004802molecular_functiontransketolase activity
A0005515molecular_functionprotein binding
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0006098biological_processpentose-phosphate shunt
A0006163biological_processpurine nucleotide metabolic process
A0016740molecular_functiontransferase activity
A0046872molecular_functionmetal ion binding
B0003824molecular_functioncatalytic activity
B0004802molecular_functiontransketolase activity
B0005515molecular_functionprotein binding
B0005737cellular_componentcytoplasm
B0005829cellular_componentcytosol
B0006098biological_processpentose-phosphate shunt
B0006163biological_processpurine nucleotide metabolic process
B0016740molecular_functiontransferase activity
B0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CA A 1681
ChainResidue
AASP157
AASN187
AILE189
ATHD1682
AHOH2140

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CA B 1681
ChainResidue
BASP157
BASP185
BASN187
BTHD1682

site_idAC3
Number of Residues24
DetailsBINDING SITE FOR RESIDUE THD A 1682
ChainResidue
AALA33
AHIS69
AHIS103
AGLY116
APRO117
ALEU118
AASP157
AGLY158
AGLU162
AASN187
AILE189
AILE191
AHIS263
ACA1681
AHOH2049
AHOH2404
AHOH2405
BASP382
BILE416
BGLU418
BPHE442
BPHE445
BTYR448
BHIS481

site_idAC4
Number of Residues23
DetailsBINDING SITE FOR RESIDUE THD B 1682
ChainResidue
AASP382
AGLU418
APHE442
APHE445
ATYR448
AHIS481
BALA33
BHIS69
BHIS103
BGLY116
BLEU118
BASP157
BGLY158
BGLU162
BASN187
BILE189
BTHR190
BILE191
BHIS263
BCA1681
BHOH2027
BHOH2058
BHOH2454

Functional Information from PROSITE/UniProt
site_idPS00801
Number of Residues21
DetailsTRANSKETOLASE_1 Transketolase signature 1. RilaVDtvskanSGHPGapLG
ChainResidueDetails
AARG16-GLY36

site_idPS00802
Number of Residues17
DetailsTRANSKETOLASE_2 Transketolase signature 2. GEDGPTHqPIEtlAhfR
ChainResidueDetails
AGLY475-ARG491

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Proton donor => ECO:0000305
ChainResidueDetails
AGLU418
BGLU418

site_idSWS_FT_FI2
Number of Residues16
DetailsBINDING:
ChainResidueDetails
AHIS30
BASP157
BILE189
BARG359
BSER386
BHIS469
BASP477
BARG528
AASP157
AILE189
AARG359
ASER386
AHIS469
AASP477
AARG528
BHIS30

site_idSWS_FT_FI3
Number of Residues14
DetailsBINDING: BINDING => ECO:0000269|PubMed:8176731, ECO:0000269|PubMed:8999873, ECO:0000269|PubMed:9398292
ChainResidueDetails
AHIS69
BGLY158
BASN187
BHIS263
BGLU418
BPHE445
AGLY116
AGLY158
AASN187
AHIS263
AGLU418
APHE445
BHIS69
BGLY116

site_idSWS_FT_FI4
Number of Residues4
DetailsSITE: Important for catalytic activity => ECO:0000269|PubMed:9398292
ChainResidueDetails
AHIS30
AHIS263
BHIS30
BHIS263

site_idSWS_FT_FI5
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:19779198
ChainResidueDetails
ASER286
BSER286

site_idSWS_FT_FI6
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:17330950, ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198
ChainResidueDetails
ASER335
BSER335

site_idSWS_FT_FI7
Number of Residues4
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:18407956
ChainResidueDetails
ASER402
ASER492
BSER402
BSER492

site_idSWS_FT_FI8
Number of Residues4
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0007744|PubMed:22106047
ChainResidueDetails
ALYS647
BLYS647

Catalytic Information from CSA
site_idCSA1
Number of Residues1
DetailsAnnotated By Reference To The Literature 1dtw
ChainResidueDetails
ASER254

site_idCSA10
Number of Residues1
DetailsAnnotated By Reference To The Literature 1dtw
ChainResidueDetails
BHIS260

site_idCSA2
Number of Residues1
DetailsAnnotated By Reference To The Literature 1dtw
ChainResidueDetails
BSER254

site_idCSA3
Number of Residues1
DetailsAnnotated By Reference To The Literature 1dtw
ChainResidueDetails
AGLU418

site_idCSA4
Number of Residues1
DetailsAnnotated By Reference To The Literature 1dtw
ChainResidueDetails
BGLU418

site_idCSA5
Number of Residues2
DetailsAnnotated By Reference To The Literature 1dtw
ChainResidueDetails
AGLU418
AHIS481

site_idCSA6
Number of Residues2
DetailsAnnotated By Reference To The Literature 1dtw
ChainResidueDetails
BGLU418
BHIS481

site_idCSA7
Number of Residues2
DetailsAnnotated By Reference To The Literature 1dtw
ChainResidueDetails
AHIS30
AHIS263

site_idCSA8
Number of Residues2
DetailsAnnotated By Reference To The Literature 1dtw
ChainResidueDetails
BHIS30
BHIS263

site_idCSA9
Number of Residues1
DetailsAnnotated By Reference To The Literature 1dtw
ChainResidueDetails
AHIS260

site_idMCSA1
Number of Residues4
DetailsM-CSA 219
ChainResidueDetails
AHIS30activator, hydrogen bond donor, steric role
AHIS263hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
AGLU418hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
AHIS481electrostatic stabiliser, hydrogen bond acceptor

site_idMCSA2
Number of Residues4
DetailsM-CSA 219
ChainResidueDetails
BHIS30activator, hydrogen bond donor, steric role
BHIS263hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
BGLU418hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
BHIS481electrostatic stabiliser, hydrogen bond acceptor

222036

PDB entries from 2024-07-03

PDB statisticsPDBj update infoContact PDBjnumon