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2E1D

Crystal structure of mouse transaldolase

Functional Information from GO Data
ChainGOidnamespacecontents
A0004801molecular_functiontransaldolase activity
A0005634cellular_componentnucleus
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0005975biological_processcarbohydrate metabolic process
A0006002biological_processfructose 6-phosphate metabolic process
A0006098biological_processpentose-phosphate shunt
A0009052biological_processpentose-phosphate shunt, non-oxidative branch
A0016740molecular_functiontransferase activity
A0019682biological_processglyceraldehyde-3-phosphate metabolic process
A0030246molecular_functioncarbohydrate binding
A0048029molecular_functionmonosaccharide binding
B0004801molecular_functiontransaldolase activity
B0005634cellular_componentnucleus
B0005737cellular_componentcytoplasm
B0005829cellular_componentcytosol
B0005975biological_processcarbohydrate metabolic process
B0006002biological_processfructose 6-phosphate metabolic process
B0006098biological_processpentose-phosphate shunt
B0009052biological_processpentose-phosphate shunt, non-oxidative branch
B0016740molecular_functiontransferase activity
B0019682biological_processglyceraldehyde-3-phosphate metabolic process
B0030246molecular_functioncarbohydrate binding
B0048029molecular_functionmonosaccharide binding
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SO3 A 3016
ChainResidue
AARG192
ASER237
AARG239
AHOH3128
AHOH3262

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO3 B 3017
ChainResidue
BARG192
BSER237
BARG239
BHOH3376

Functional Information from PROSITE/UniProt
site_idPS00958
Number of Residues18
DetailsTRANSALDOLASE_2 Transaldolase active site. IlIKLSsTwEGIqAgKeL
ChainResidueDetails
AILE139-LEU156

site_idPS01054
Number of Residues9
DetailsTRANSALDOLASE_1 Transaldolase signature 1. DATTNPSLI
ChainResidueDetails
AASP41-ILE49

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsActive site: {"description":"Schiff-base intermediate with substrate","evidences":[{"source":"UniProtKB","id":"P37837","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues4
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"23806337","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues6
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"P37837","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues2
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"21183079","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues2
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P37837","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idCSA1
Number of Residues3
DetailsAnnotated By Reference To The Literature 1onr
ChainResidueDetails
ALYS142
AGLU106
AASP27

site_idCSA2
Number of Residues3
DetailsAnnotated By Reference To The Literature 1onr
ChainResidueDetails
BLYS142
BGLU106
BASP27

239803

PDB entries from 2025-08-06

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