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4IQ8

Crystal structure of glyceraldehyde-3-phosphate dehydrogenase 3 from Saccharomyces cerevisiae

Functional Information from GO Data
ChainGOidnamespacecontents
A0003723molecular_functionRNA binding
A0003729molecular_functionmRNA binding
A0004365molecular_functionglyceraldehyde-3-phosphate dehydrogenase (NAD+) (phosphorylating) activity
A0005634cellular_componentnucleus
A0005737cellular_componentcytoplasm
A0005739cellular_componentmitochondrion
A0005811cellular_componentlipid droplet
A0005829cellular_componentcytosol
A0005886cellular_componentplasma membrane
A0006006biological_processglucose metabolic process
A0006094biological_processgluconeogenesis
A0006096biological_processglycolytic process
A0006915biological_processapoptotic process
A0009277cellular_componentfungal-type cell wall
A0015886biological_processheme transport
A0016491molecular_functionoxidoreductase activity
A0016620molecular_functionoxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor
A0020037molecular_functionheme binding
A0030312cellular_componentexternal encapsulating structure
A0050661molecular_functionNADP binding
A0051287molecular_functionNAD binding
A0072593biological_processreactive oxygen species metabolic process
A1904408molecular_functionmelatonin binding
Functional Information from PROSITE/UniProt
site_idPS00071
Number of Residues8
DetailsGAPDH Glyceraldehyde 3-phosphate dehydrogenase active site. ASCTTNcL
ChainResidueDetails
AALA148-LEU155

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Nucleophile => ECO:0000255|PROSITE-ProRule:PRU10009
ChainResidueDetails
ACYS150

site_idSWS_FT_FI2
Number of Residues6
DetailsBINDING: BINDING => ECO:0007744|PDB:3PYM
ChainResidueDetails
AARG11
AILE12
AASP33
ATHR120
AASN314
ATYR318

site_idSWS_FT_FI3
Number of Residues4
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:P22513
ChainResidueDetails
ASER149
ATHR180
ATHR209
AARG232

site_idSWS_FT_FI4
Number of Residues1
DetailsSITE: Activates thiol group during catalysis => ECO:0000250|UniProtKB:P04406
ChainResidueDetails
AHIS177

site_idSWS_FT_FI5
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:18407956
ChainResidueDetails
ASER302

site_idSWS_FT_FI6
Number of Residues3
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0007744|PubMed:22106047
ChainResidueDetails
ALYS46
ALYS63

223532

PDB entries from 2024-08-07

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