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1NGS

COMPLEX OF TRANSKETOLASE WITH THIAMIN DIPHOSPHATE, CA2+ AND ACCEPTOR SUBSTRATE ERYTHROSE-4-PHOSPHATE

Functional Information from GO Data
ChainGOidnamespacecontents
A0003824molecular_functioncatalytic activity
A0004802molecular_functiontransketolase activity
A0005515molecular_functionprotein binding
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0006098biological_processpentose-phosphate shunt
A0016740molecular_functiontransferase activity
A0046872molecular_functionmetal ion binding
B0003824molecular_functioncatalytic activity
B0004802molecular_functiontransketolase activity
B0005515molecular_functionprotein binding
B0005737cellular_componentcytoplasm
B0005829cellular_componentcytosol
B0006098biological_processpentose-phosphate shunt
B0016740molecular_functiontransferase activity
B0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CA A 681
ChainResidue
AASP157
AASN187
AILE189
ATPP682

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CA B 681
ChainResidue
BASP157
BASN187
BILE189
BTPP682

site_idAC3
Number of Residues8
DetailsBINDING SITE FOR RESIDUE E4P A 900
ChainResidue
AHIS263
AGLY264
ATPP682
BSER386
BHIS469
BASP477
BARG528
AHIS30

site_idAC4
Number of Residues22
DetailsBINDING SITE FOR RESIDUE TPP A 682
ChainResidue
AHIS69
AGLY116
APRO117
ALEU118
AGLY156
AASP157
AGLY158
AGLU162
AASN187
AILE189
ATHR190
AILE191
AHIS263
ACA681
AE4P900
AHOH932
BASP382
BILE416
BGLU418
BPHE445
BTYR448
BHIS481

site_idAC5
Number of Residues9
DetailsBINDING SITE FOR RESIDUE E4P B 900
ChainResidue
ASER386
AHIS469
AASP477
AARG528
AHOH1057
BHIS30
BILE191
BHIS263
BTPP682

site_idAC6
Number of Residues20
DetailsBINDING SITE FOR RESIDUE TPP B 682
ChainResidue
AASP382
AGLU418
APHE445
ATYR448
BALA33
BHIS69
BGLY116
BPRO117
BLEU118
BGLY158
BGLU162
BASN187
BILE189
BTHR190
BILE191
BILE250
BHIS263
BCA681
BE4P900
BHOH923

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
AHIS419
BHIS419

site_idSWS_FT_FI2
Number of Residues16
DetailsBINDING:
ChainResidueDetails
APRO31
BGLY158
BTHR190
BLYS360
BASN387
BASP470
BGLY478
BGLN529
AGLY158
ATHR190
ALYS360
AASN387
AASP470
AGLY478
AGLN529
BPRO31

site_idSWS_FT_FI3
Number of Residues14
DetailsBINDING: BINDING => ECO:0000269|PubMed:8176731, ECO:0000269|PubMed:8999873, ECO:0000269|PubMed:9398292
ChainResidueDetails
AALA70
BCYS159
BLYS188
BGLY264
BHIS419
BVAL446
APRO117
ACYS159
ALYS188
AGLY264
AHIS419
AVAL446
BALA70
BPRO117

site_idSWS_FT_FI4
Number of Residues4
DetailsSITE: Important for catalytic activity => ECO:0000269|PubMed:9398292
ChainResidueDetails
APRO31
AGLY264
BPRO31
BGLY264

site_idSWS_FT_FI5
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:19779198
ChainResidueDetails
APHE287
BPHE287

site_idSWS_FT_FI6
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:17330950, ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198
ChainResidueDetails
AGLY336
BGLY336

site_idSWS_FT_FI7
Number of Residues4
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:18407956
ChainResidueDetails
AGLY403
ALEU493
BGLY403
BLEU493

site_idSWS_FT_FI8
Number of Residues4
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0007744|PubMed:22106047
ChainResidueDetails
APHE648
BPHE648

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
APRO31activator, hydrogen bond donor, steric role
AGLY264hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
AHIS419hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
AGLN482electrostatic stabiliser, hydrogen bond acceptor

site_idMCSA2
Number of Residues4
DetailsM-CSA 219
ChainResidueDetails
BPRO31activator, hydrogen bond donor, steric role
BGLY264hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
BHIS419hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
BGLN482electrostatic stabiliser, hydrogen bond acceptor

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PDB entries from 2024-11-06

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