3LC2
Crystal Structure of Thioacyl-Glyceraldehyde-3-phosphate dehydrogenase 1(GAPDH 1) from methicillin resistant Staphylococcus aureus MRSA252
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 | 6 |
Details | BINDING SITE FOR RESIDUE G3H O 337 |
Chain | Residue |
O | SER150 |
O | CYS151 |
O | THR152 |
O | HIS178 |
O | THR211 |
O | GLY212 |
site_id | AC2 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE GOL O 339 |
Chain | Residue |
O | GLY11 |
O | ARG12 |
site_id | AC3 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE G3H Q 337 |
Chain | Residue |
Q | CYS151 |
Q | THR152 |
Q | HIS178 |
Q | THR211 |
Q | GLY212 |
Q | HOH350 |
Q | SER150 |
site_id | AC4 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE GOL Q 339 |
Chain | Residue |
Q | GLY11 |
Q | ARG12 |
Q | HOH352 |
site_id | AC5 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE G3H R 337 |
Chain | Residue |
R | SER150 |
R | CYS151 |
R | THR152 |
R | HIS178 |
R | THR181 |
R | THR211 |
R | GLY212 |
site_id | AC6 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE GOL R 339 |
Chain | Residue |
R | GLY11 |
R | ARG12 |
R | ILE13 |
R | HOH374 |
site_id | AC7 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE G3H P 337 |
Chain | Residue |
P | SER150 |
P | CYS151 |
P | THR152 |
P | HIS178 |
P | THR181 |
P | THR211 |
P | GLY212 |
P | HOH363 |
P | HOH370 |
Functional Information from PROSITE/UniProt
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 |
O | CYS151 | |
Q | CYS151 | |
R | CYS151 | |
P | CYS151 |
site_id | SWS_FT_FI2 |
Number of Residues | 12 |
Details | BINDING: BINDING => ECO:0000269|PubMed:20620151, ECO:0000269|Ref.3 |
Chain | Residue | Details |
O | ARG12 | |
P | ARG12 | |
P | ASP34 | |
P | SER120 | |
O | ASP34 | |
O | SER120 | |
Q | ARG12 | |
Q | ASP34 | |
Q | SER120 | |
R | ARG12 | |
R | ASP34 | |
R | SER120 |
site_id | SWS_FT_FI3 |
Number of Residues | 20 |
Details | BINDING: BINDING => ECO:0000269|PubMed:20620151 |
Chain | Residue | Details |
O | SER150 | |
Q | ASN316 | |
R | SER150 | |
R | THR181 | |
R | THR211 | |
R | ARG234 | |
R | ASN316 | |
P | SER150 | |
P | THR181 | |
P | THR211 | |
P | ARG234 | |
O | THR181 | |
P | ASN316 | |
O | THR211 | |
O | ARG234 | |
O | ASN316 | |
Q | SER150 | |
Q | THR181 | |
Q | THR211 | |
Q | ARG234 |
site_id | SWS_FT_FI4 |
Number of Residues | 4 |
Details | BINDING: BINDING => ECO:0000250|UniProtKB:P00362 |
Chain | Residue | Details |
O | ARG198 | |
Q | ARG198 | |
R | ARG198 | |
P | ARG198 |
site_id | SWS_FT_FI5 |
Number of Residues | 4 |
Details | SITE: Activates thiol group during catalysis => ECO:0000269|PubMed:20620151 |
Chain | Residue | Details |
O | HIS178 | |
Q | HIS178 | |
R | HIS178 | |
P | HIS178 |