3LVF
Crystal Structure of holo Glyceraldehyde-3-phosphate dehydrogenase 1 (GAPDH1) from methicillin resistant Staphylococcus aureus MRSA252 at 1.7 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 | 32 |
Details | BINDING SITE FOR RESIDUE NAD P 337 |
Chain | Residue |
P | GLY9 |
P | CYS96 |
P | THR97 |
P | GLY98 |
P | PHE99 |
P | SER120 |
P | ALA121 |
P | ASN316 |
P | TYR320 |
P | HOH341 |
P | HOH344 |
P | GLY11 |
P | HOH351 |
P | HOH368 |
P | HOH372 |
P | HOH377 |
P | HOH407 |
P | HOH427 |
P | HOH429 |
P | HOH430 |
P | HOH510 |
P | HOH566 |
P | ARG12 |
P | HOH576 |
Q | PRO190 |
Q | HOH342 |
P | ILE13 |
P | ASN33 |
P | ASP34 |
P | LEU35 |
P | GLU77 |
P | PRO78 |
site_id | AC2 |
Number of Residues | 32 |
Details | BINDING SITE FOR RESIDUE NAD R 337 |
Chain | Residue |
O | PRO190 |
O | HOH372 |
R | GLY9 |
R | GLY11 |
R | ARG12 |
R | ILE13 |
R | ASN33 |
R | ASP34 |
R | LEU35 |
R | PRO78 |
R | CYS96 |
R | THR97 |
R | GLY98 |
R | PHE99 |
R | SER120 |
R | ALA121 |
R | THR181 |
R | ASN316 |
R | TYR320 |
R | HOH340 |
R | HOH342 |
R | HOH354 |
R | HOH387 |
R | HOH423 |
R | HOH433 |
R | HOH446 |
R | HOH449 |
R | HOH451 |
R | HOH454 |
R | HOH591 |
R | HOH618 |
R | HOH658 |
site_id | AC3 |
Number of Residues | 30 |
Details | BINDING SITE FOR RESIDUE NAD O 337 |
Chain | Residue |
O | GLY9 |
O | GLY11 |
O | ARG12 |
O | ILE13 |
O | ASN33 |
O | ASP34 |
O | PRO78 |
O | CYS96 |
O | THR97 |
O | GLY98 |
O | SER120 |
O | ALA121 |
O | ASN316 |
O | TYR320 |
O | HOH343 |
O | HOH344 |
O | HOH348 |
O | HOH350 |
O | HOH362 |
O | HOH366 |
O | HOH384 |
O | HOH386 |
O | HOH419 |
O | HOH421 |
O | HOH434 |
O | HOH437 |
O | HOH449 |
O | HOH503 |
R | PRO190 |
R | HOH338 |
site_id | AC4 |
Number of Residues | 31 |
Details | BINDING SITE FOR RESIDUE NAD Q 337 |
Chain | Residue |
Q | ILE13 |
Q | ASN33 |
Q | ASP34 |
Q | LEU35 |
Q | GLU77 |
Q | PRO78 |
Q | CYS96 |
Q | THR97 |
Q | GLY98 |
Q | PHE99 |
Q | SER120 |
Q | ALA121 |
Q | ASN316 |
Q | TYR320 |
Q | HOH357 |
Q | HOH365 |
Q | HOH370 |
Q | HOH380 |
Q | HOH382 |
Q | HOH391 |
Q | HOH404 |
Q | HOH421 |
Q | HOH461 |
Q | HOH527 |
Q | HOH589 |
Q | HOH688 |
P | PRO190 |
P | HOH406 |
Q | GLY9 |
Q | GLY11 |
Q | ARG12 |
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 |
P | CYS151 | |
R | CYS151 | |
O | CYS151 | |
Q | CYS151 |
site_id | SWS_FT_FI2 |
Number of Residues | 12 |
Details | BINDING: BINDING => ECO:0000269|PubMed:20620151, ECO:0000269|Ref.3 |
Chain | Residue | Details |
P | ARG12 | |
Q | ARG12 | |
Q | ASP34 | |
Q | SER120 | |
P | ASP34 | |
P | SER120 | |
R | ARG12 | |
R | ASP34 | |
R | SER120 | |
O | ARG12 | |
O | ASP34 | |
O | SER120 |
site_id | SWS_FT_FI3 |
Number of Residues | 20 |
Details | BINDING: BINDING => ECO:0000269|PubMed:20620151 |
Chain | Residue | Details |
P | SER150 | |
R | ASN316 | |
O | SER150 | |
O | THR181 | |
O | THR211 | |
O | ARG234 | |
O | ASN316 | |
Q | SER150 | |
Q | THR181 | |
Q | THR211 | |
Q | ARG234 | |
P | THR181 | |
Q | ASN316 | |
P | THR211 | |
P | ARG234 | |
P | ASN316 | |
R | SER150 | |
R | THR181 | |
R | THR211 | |
R | ARG234 |
site_id | SWS_FT_FI4 |
Number of Residues | 4 |
Details | BINDING: BINDING => ECO:0000250|UniProtKB:P00362 |
Chain | Residue | Details |
P | ARG198 | |
R | ARG198 | |
O | ARG198 | |
Q | ARG198 |
site_id | SWS_FT_FI5 |
Number of Residues | 4 |
Details | SITE: Activates thiol group during catalysis => ECO:0000269|PubMed:20620151 |
Chain | Residue | Details |
P | HIS178 | |
R | HIS178 | |
O | HIS178 | |
Q | HIS178 |