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
Chain | GOid | namespace | contents |
O | 0000166 | molecular_function | nucleotide binding |
O | 0004365 | molecular_function | glyceraldehyde-3-phosphate dehydrogenase (NAD+) (phosphorylating) activity |
O | 0005737 | cellular_component | cytoplasm |
O | 0006006 | biological_process | glucose metabolic process |
O | 0006096 | biological_process | glycolytic process |
O | 0016491 | molecular_function | oxidoreductase activity |
O | 0016620 | molecular_function | oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor |
O | 0030554 | molecular_function | adenyl nucleotide binding |
O | 0050661 | molecular_function | NADP binding |
O | 0051287 | molecular_function | NAD binding |
P | 0000166 | molecular_function | nucleotide binding |
P | 0004365 | molecular_function | glyceraldehyde-3-phosphate dehydrogenase (NAD+) (phosphorylating) activity |
P | 0005737 | cellular_component | cytoplasm |
P | 0006006 | biological_process | glucose metabolic process |
P | 0006096 | biological_process | glycolytic process |
P | 0016491 | molecular_function | oxidoreductase activity |
P | 0016620 | molecular_function | oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor |
P | 0030554 | molecular_function | adenyl nucleotide binding |
P | 0050661 | molecular_function | NADP binding |
P | 0051287 | molecular_function | NAD binding |
Q | 0000166 | molecular_function | nucleotide binding |
Q | 0004365 | molecular_function | glyceraldehyde-3-phosphate dehydrogenase (NAD+) (phosphorylating) activity |
Q | 0005737 | cellular_component | cytoplasm |
Q | 0006006 | biological_process | glucose metabolic process |
Q | 0006096 | biological_process | glycolytic process |
Q | 0016491 | molecular_function | oxidoreductase activity |
Q | 0016620 | molecular_function | oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor |
Q | 0030554 | molecular_function | adenyl nucleotide binding |
Q | 0050661 | molecular_function | NADP binding |
Q | 0051287 | molecular_function | NAD binding |
R | 0000166 | molecular_function | nucleotide binding |
R | 0004365 | molecular_function | glyceraldehyde-3-phosphate dehydrogenase (NAD+) (phosphorylating) activity |
R | 0005737 | cellular_component | cytoplasm |
R | 0006006 | biological_process | glucose metabolic process |
R | 0006096 | biological_process | glycolytic process |
R | 0016491 | molecular_function | oxidoreductase activity |
R | 0016620 | molecular_function | oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor |
R | 0030554 | molecular_function | adenyl nucleotide binding |
R | 0050661 | molecular_function | NADP binding |
R | 0051287 | molecular_function | NAD binding |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 24 |
Details | BINDING SITE FOR RESIDUE NAD Q 0 |
Chain | Residue |
P | PRO190 |
Q | CYS96 |
Q | THR97 |
Q | GLY98 |
Q | SER120 |
Q | ALA121 |
Q | THR181 |
Q | ASN316 |
Q | TYR320 |
Q | GOL337 |
Q | HOH341 |
Q | GLY9 |
Q | HOH342 |
Q | HOH347 |
Q | HOH413 |
Q | HOH421 |
Q | HOH425 |
Q | GLY11 |
Q | ARG12 |
Q | ILE13 |
Q | ASN33 |
Q | ASP34 |
Q | LEU35 |
Q | PRO78 |
site_id | AC2 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE GOL Q 337 |
Chain | Residue |
Q | NAD0 |
Q | SER150 |
Q | GLY151 |
Q | THR152 |
Q | HIS178 |
Q | THR211 |
Q | HOH425 |
site_id | AC3 |
Number of Residues | 24 |
Details | BINDING SITE FOR RESIDUE NAD O 0 |
Chain | Residue |
O | GLY9 |
O | GLY11 |
O | ARG12 |
O | ILE13 |
O | ASN33 |
O | ASP34 |
O | PRO78 |
O | CYS96 |
O | THR97 |
O | GLY98 |
O | PHE99 |
O | SER120 |
O | ALA121 |
O | ASN316 |
O | TYR320 |
O | GOL337 |
O | CL338 |
O | HOH358 |
O | HOH366 |
O | HOH373 |
O | HOH381 |
O | HOH393 |
R | PRO190 |
R | HOH342 |
site_id | AC4 |
Number of Residues | 10 |
Details | BINDING SITE FOR RESIDUE GOL O 337 |
Chain | Residue |
O | NAD0 |
O | ARG12 |
O | TYR180 |
O | THR181 |
O | GLY182 |
O | ALA238 |
O | THR239 |
O | ASN316 |
O | GLU317 |
R | GLN187 |
site_id | AC5 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE CL O 338 |
Chain | Residue |
O | NAD0 |
O | THR181 |
site_id | AC6 |
Number of Residues | 24 |
Details | BINDING SITE FOR RESIDUE NAD P 0 |
Chain | Residue |
P | GLY9 |
P | GLY11 |
P | ARG12 |
P | ILE13 |
P | ASN33 |
P | ASP34 |
P | PRO78 |
P | CYS96 |
P | THR97 |
P | GLY98 |
P | PHE99 |
P | SER120 |
P | ALA121 |
P | THR181 |
P | ASN316 |
P | TYR320 |
P | GOL337 |
P | HOH338 |
P | HOH339 |
P | HOH370 |
P | HOH372 |
P | HOH395 |
P | HOH396 |
Q | PRO190 |
site_id | AC7 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE GOL P 337 |
Chain | Residue |
P | NAD0 |
P | SER150 |
P | GLY151 |
P | THR152 |
P | HIS178 |
P | TYR314 |
P | HOH394 |
site_id | AC8 |
Number of Residues | 20 |
Details | BINDING SITE FOR RESIDUE NAD R 0 |
Chain | Residue |
O | HOH430 |
R | GLY9 |
R | GLY11 |
R | ARG12 |
R | ILE13 |
R | ASN33 |
R | ASP34 |
R | PRO78 |
R | CYS96 |
R | THR97 |
R | GLY98 |
R | PHE99 |
R | SER120 |
R | ALA121 |
R | ASN316 |
R | TYR320 |
R | HOH356 |
R | HOH359 |
R | HOH378 |
O | PRO190 |
Functional Information from PROSITE/UniProt
site_id | PS00211 |
Number of Residues | 15 |
Details | ABC_TRANSPORTER_1 ABC transporters family signature. MSVGDRQLVKVAAWY |
Chain | Residue | Details |
Q | MET300-TYR314 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 4 |
Details | ACT_SITE: Nucleophile => ECO:0000269|PubMed:20620151 |
Chain | Residue | Details |
Q | GLY151 | |
O | GLY151 | |
P | GLY151 | |
R | GLY151 |
site_id | SWS_FT_FI2 |
Number of Residues | 12 |
Details | BINDING: BINDING => ECO:0000269|PubMed:20620151, ECO:0000269|Ref.3 |
Chain | Residue | Details |
Q | ARG12 | |
R | ARG12 | |
R | ASP34 | |
R | SER120 | |
Q | ASP34 | |
Q | SER120 | |
O | ARG12 | |
O | ASP34 | |
O | SER120 | |
P | ARG12 | |
P | ASP34 | |
P | SER120 |
site_id | SWS_FT_FI3 |
Number of Residues | 20 |
Details | BINDING: BINDING => ECO:0000269|PubMed:20620151 |
Chain | Residue | Details |
Q | SER150 | |
O | ASN316 | |
P | SER150 | |
P | THR181 | |
P | THR211 | |
P | ARG234 | |
P | ASN316 | |
R | SER150 | |
R | THR181 | |
R | THR211 | |
R | ARG234 | |
Q | THR181 | |
R | ASN316 | |
Q | THR211 | |
Q | ARG234 | |
Q | ASN316 | |
O | SER150 | |
O | THR181 | |
O | THR211 | |
O | ARG234 |
site_id | SWS_FT_FI4 |
Number of Residues | 4 |
Details | BINDING: BINDING => ECO:0000250|UniProtKB:P00362 |
Chain | Residue | Details |
Q | ARG198 | |
O | ARG198 | |
P | ARG198 | |
R | ARG198 |
site_id | SWS_FT_FI5 |
Number of Residues | 4 |
Details | SITE: Activates thiol group during catalysis => ECO:0000269|PubMed:20620151 |
Chain | Residue | Details |
Q | HIS178 | |
O | HIS178 | |
P | HIS178 | |
R | HIS178 |