Loading
PDBj
MenuPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDBDonate
RCSB PDBPDBeBMRBAdv. SearchSearch help

3L6O

Crystal Structure of Phosphate bound apo Glyceraldehyde-3-phosphate dehydrogenase 1 from MRSA252 at 2.2 Angstrom resolution

Functional Information from GO Data
ChainGOidnamespacecontents
O0000166molecular_functionnucleotide binding
O0004365molecular_functionglyceraldehyde-3-phosphate dehydrogenase (NAD+) (phosphorylating) activity
O0005737cellular_componentcytoplasm
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
O0050661molecular_functionNADP binding
O0051287molecular_functionNAD binding
P0000166molecular_functionnucleotide binding
P0004365molecular_functionglyceraldehyde-3-phosphate dehydrogenase (NAD+) (phosphorylating) activity
P0005737cellular_componentcytoplasm
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
P0050661molecular_functionNADP binding
P0051287molecular_functionNAD binding
Q0000166molecular_functionnucleotide binding
Q0004365molecular_functionglyceraldehyde-3-phosphate dehydrogenase (NAD+) (phosphorylating) activity
Q0005737cellular_componentcytoplasm
Q0006006biological_processglucose metabolic process
Q0006096biological_processglycolytic process
Q0016491molecular_functionoxidoreductase activity
Q0016620molecular_functionoxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor
Q0050661molecular_functionNADP binding
Q0051287molecular_functionNAD binding
R0000166molecular_functionnucleotide binding
R0004365molecular_functionglyceraldehyde-3-phosphate dehydrogenase (NAD+) (phosphorylating) activity
R0005737cellular_componentcytoplasm
R0006006biological_processglucose metabolic process
R0006096biological_processglycolytic process
R0016491molecular_functionoxidoreductase activity
R0016620molecular_functionoxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor
R0050661molecular_functionNADP binding
R0051287molecular_functionNAD binding
Functional Information from PDB Data
site_idAC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE PO4 R 337
ChainResidue
RSER150
RCYS151
RTHR152
RHIS178
RTHR211
RGLY212

site_idAC2
Number of Residues7
DetailsBINDING SITE FOR RESIDUE PO4 P 337
ChainResidue
PHIS178
PTHR211
PGLY212
PHOH369
PSER150
PCYS151
PTHR152

site_idAC3
Number of Residues7
DetailsBINDING SITE FOR RESIDUE PO4 O 337
ChainResidue
OSER150
OCYS151
OTHR152
OHIS178
OTHR211
OGLY212
OHOH339

site_idAC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE PO4 Q 337
ChainResidue
QSER150
QCYS151
QTHR152
QHIS178
QTHR211
QGLY212

Functional Information from PROSITE/UniProt
site_idPS00071
Number of Residues8
DetailsGAPDH Glyceraldehyde 3-phosphate dehydrogenase active site. ASCTTNsL
ChainResidueDetails
QALA149-LEU156

site_idPS00211
Number of Residues15
DetailsABC_TRANSPORTER_1 ABC transporters family signature. MSVGDRQLVKVAAWY
ChainResidueDetails
QMET300-TYR314

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsACT_SITE: Nucleophile => ECO:0000269|PubMed:20620151
ChainResidueDetails
QCYS151
PCYS151
RCYS151
OCYS151

site_idSWS_FT_FI2
Number of Residues12
DetailsBINDING: BINDING => ECO:0000269|PubMed:20620151, ECO:0000269|Ref.3
ChainResidueDetails
QARG12
OARG12
OASP34
OSER120
QASP34
QSER120
PARG12
PASP34
PSER120
RARG12
RASP34
RSER120

site_idSWS_FT_FI3
Number of Residues20
DetailsBINDING: BINDING => ECO:0000269|PubMed:20620151
ChainResidueDetails
QSER150
PASN316
RSER150
RTHR181
RTHR211
RARG234
RASN316
OSER150
OTHR181
OTHR211
OARG234
QTHR181
OASN316
QTHR211
QARG234
QASN316
PSER150
PTHR181
PTHR211
PARG234

site_idSWS_FT_FI4
Number of Residues4
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:P00362
ChainResidueDetails
QARG198
PARG198
RARG198
OARG198

site_idSWS_FT_FI5
Number of Residues4
DetailsSITE: Activates thiol group during catalysis => ECO:0000269|PubMed:20620151
ChainResidueDetails
QHIS178
PHIS178
RHIS178
OHIS178

237735

PDB entries from 2025-06-18

PDB statisticsPDBj update infoContact PDBjnumon