Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

3K9Q

Crystal structure of C151G mutant of Glyceraldehyde 3-phosphate dehydrogenase 1 from Methicillin resistant Staphylococcus aureus (MRSA252) at 2.5 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
O0030554molecular_functionadenyl nucleotide binding
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
P0030554molecular_functionadenyl nucleotide binding
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
Q0030554molecular_functionadenyl nucleotide binding
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
R0030554molecular_functionadenyl nucleotide binding
R0050661molecular_functionNADP binding
R0051287molecular_functionNAD binding
Functional Information from PDB Data
site_idAC1
Number of Residues24
DetailsBINDING SITE FOR RESIDUE NAD Q 0
ChainResidue
PPRO190
QCYS96
QTHR97
QGLY98
QSER120
QALA121
QTHR181
QASN316
QTYR320
QGOL337
QHOH341
QGLY9
QHOH342
QHOH347
QHOH413
QHOH421
QHOH425
QGLY11
QARG12
QILE13
QASN33
QASP34
QLEU35
QPRO78

site_idAC2
Number of Residues7
DetailsBINDING SITE FOR RESIDUE GOL Q 337
ChainResidue
QNAD0
QSER150
QGLY151
QTHR152
QHIS178
QTHR211
QHOH425

site_idAC3
Number of Residues24
DetailsBINDING SITE FOR RESIDUE NAD O 0
ChainResidue
OGLY9
OGLY11
OARG12
OILE13
OASN33
OASP34
OPRO78
OCYS96
OTHR97
OGLY98
OPHE99
OSER120
OALA121
OASN316
OTYR320
OGOL337
OCL338
OHOH358
OHOH366
OHOH373
OHOH381
OHOH393
RPRO190
RHOH342

site_idAC4
Number of Residues10
DetailsBINDING SITE FOR RESIDUE GOL O 337
ChainResidue
ONAD0
OARG12
OTYR180
OTHR181
OGLY182
OALA238
OTHR239
OASN316
OGLU317
RGLN187

site_idAC5
Number of Residues2
DetailsBINDING SITE FOR RESIDUE CL O 338
ChainResidue
ONAD0
OTHR181

site_idAC6
Number of Residues24
DetailsBINDING SITE FOR RESIDUE NAD P 0
ChainResidue
PGLY9
PGLY11
PARG12
PILE13
PASN33
PASP34
PPRO78
PCYS96
PTHR97
PGLY98
PPHE99
PSER120
PALA121
PTHR181
PASN316
PTYR320
PGOL337
PHOH338
PHOH339
PHOH370
PHOH372
PHOH395
PHOH396
QPRO190

site_idAC7
Number of Residues7
DetailsBINDING SITE FOR RESIDUE GOL P 337
ChainResidue
PNAD0
PSER150
PGLY151
PTHR152
PHIS178
PTYR314
PHOH394

site_idAC8
Number of Residues20
DetailsBINDING SITE FOR RESIDUE NAD R 0
ChainResidue
OHOH430
RGLY9
RGLY11
RARG12
RILE13
RASN33
RASP34
RPRO78
RCYS96
RTHR97
RGLY98
RPHE99
RSER120
RALA121
RASN316
RTYR320
RHOH356
RHOH359
RHOH378
OPRO190

Functional Information from PROSITE/UniProt
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
QGLY151
OGLY151
PGLY151
RGLY151

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

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

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

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

218853

PDB entries from 2024-04-24

PDB statisticsPDBj update infoContact PDBjnumon