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2I5P

Crystal structure of glyceraldehyde-3-phosphate dehydrogenase isoform 1 from K. marxianus

Functional Information from GO Data
ChainGOidnamespacecontents
O0004365molecular_functionglyceraldehyde-3-phosphate dehydrogenase (NAD+) (phosphorylating) activity
O0005737cellular_componentcytoplasm
O0005829cellular_componentcytosol
O0006006biological_processglucose metabolic process
O0006096biological_processglycolytic process
O0016491molecular_functionoxidoreductase activity
O0016620molecular_functionoxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor
O0030312cellular_componentexternal encapsulating structure
O0050661molecular_functionNADP binding
O0051287molecular_functionNAD binding
P0004365molecular_functionglyceraldehyde-3-phosphate dehydrogenase (NAD+) (phosphorylating) activity
P0005737cellular_componentcytoplasm
P0005829cellular_componentcytosol
P0006006biological_processglucose metabolic process
P0006096biological_processglycolytic process
P0016491molecular_functionoxidoreductase activity
P0016620molecular_functionoxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor
P0030312cellular_componentexternal encapsulating structure
P0050661molecular_functionNADP binding
P0051287molecular_functionNAD binding
Functional Information from PROSITE/UniProt
site_idPS00071
Number of Residues8
DetailsGAPDH Glyceraldehyde 3-phosphate dehydrogenase active site. ASCTTNcL
ChainResidueDetails
OALA147-LEU154

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Nucleophile => ECO:0000250|UniProtKB:P22513, ECO:0000255|PROSITE-ProRule:PRU10009
ChainResidueDetails
OCYS149
PCYS649

site_idSWS_FT_FI2
Number of Residues16
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:P22513
ChainResidueDetails
OGLU76
OSER148
OTHR179
OTHR208
OARG231
OASN313
PARG510
PASP532
PGLU576
PSER648
PTHR679
PTHR708
PARG731
PASN813
OARG10
OASP32

site_idSWS_FT_FI3
Number of Residues2
DetailsSITE: Activates thiol group during catalysis => ECO:0000250|UniProtKB:P22513
ChainResidueDetails
OHIS176
PHIS676

site_idSWS_FT_FI4
Number of Residues6
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P00359
ChainResidueDetails
OSER200
PSER648
PSER677
PSER700
OSER148
OSER177

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PDB entries from 2024-05-29

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