3RHH
Crystal structure of NADP-dependent glyceraldehyde-3-phosphate dehydrogenase from Bacillus halodurans C-125 complexed with NADP
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0000166 | molecular_function | nucleotide binding |
A | 0008886 | molecular_function | glyceraldehyde-3-phosphate dehydrogenase (NADP+) (non-phosphorylating) activity |
A | 0008911 | molecular_function | lactaldehyde dehydrogenase activity |
A | 0016491 | molecular_function | oxidoreductase activity |
A | 0016620 | molecular_function | oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor |
B | 0000166 | molecular_function | nucleotide binding |
B | 0008886 | molecular_function | glyceraldehyde-3-phosphate dehydrogenase (NADP+) (non-phosphorylating) activity |
B | 0008911 | molecular_function | lactaldehyde dehydrogenase activity |
B | 0016491 | molecular_function | oxidoreductase activity |
B | 0016620 | molecular_function | oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor |
C | 0000166 | molecular_function | nucleotide binding |
C | 0008886 | molecular_function | glyceraldehyde-3-phosphate dehydrogenase (NADP+) (non-phosphorylating) activity |
C | 0008911 | molecular_function | lactaldehyde dehydrogenase activity |
C | 0016491 | molecular_function | oxidoreductase activity |
C | 0016620 | molecular_function | oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor |
D | 0000166 | molecular_function | nucleotide binding |
D | 0008886 | molecular_function | glyceraldehyde-3-phosphate dehydrogenase (NADP+) (non-phosphorylating) activity |
D | 0008911 | molecular_function | lactaldehyde dehydrogenase activity |
D | 0016491 | molecular_function | oxidoreductase activity |
D | 0016620 | molecular_function | oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 13 |
Details | BINDING SITE FOR RESIDUE NAP A 506 |
Chain | Residue |
A | ILE159 |
A | PHE237 |
A | GLY240 |
A | THR243 |
A | HOH557 |
A | SER160 |
A | LYS186 |
A | PRO187 |
A | ALA188 |
A | THR189 |
A | GLY219 |
A | GLY223 |
A | ASP224 |
site_id | AC2 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE SO4 A 507 |
Chain | Residue |
A | ARG112 |
A | ARG292 |
A | GLU445 |
A | ARG446 |
A | GLY447 |
A | HOH556 |
site_id | AC3 |
Number of Residues | 18 |
Details | BINDING SITE FOR RESIDUE NAP B 506 |
Chain | Residue |
B | ILE159 |
B | SER160 |
B | PRO161 |
B | PHE162 |
B | LYS186 |
B | PRO187 |
B | ALA188 |
B | THR189 |
B | GLY217 |
B | GLY219 |
B | GLY223 |
B | ASP224 |
B | PHE237 |
B | GLY239 |
B | GLY240 |
B | THR243 |
B | HOH512 |
B | HOH560 |
site_id | AC4 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE SO4 B 507 |
Chain | Residue |
B | ARG112 |
B | TYR164 |
B | ARG446 |
B | GLY447 |
site_id | AC5 |
Number of Residues | 16 |
Details | BINDING SITE FOR RESIDUE NAP C 506 |
Chain | Residue |
C | ILE159 |
C | SER160 |
C | PHE162 |
C | LYS186 |
C | PRO187 |
C | ALA188 |
C | THR189 |
C | ARG218 |
C | GLY219 |
C | GLY223 |
C | ASP224 |
C | PHE237 |
C | GLY240 |
C | THR243 |
C | ARG246 |
C | HOH532 |
site_id | AC6 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE SO4 C 507 |
Chain | Residue |
C | ARG112 |
C | TYR164 |
C | ARG292 |
C | GLU445 |
C | ARG446 |
C | GLY447 |
site_id | AC7 |
Number of Residues | 17 |
Details | BINDING SITE FOR RESIDUE NAP D 506 |
Chain | Residue |
D | ILE159 |
D | SER160 |
D | PRO161 |
D | PHE162 |
D | LYS186 |
D | PRO187 |
D | ALA188 |
D | THR189 |
D | ARG218 |
D | GLY219 |
D | GLY223 |
D | ASP224 |
D | PHE237 |
D | GLY239 |
D | GLY240 |
D | THR243 |
D | ARG246 |
site_id | AC8 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE SO4 D 507 |
Chain | Residue |
D | ARG112 |
D | TYR164 |
D | ARG292 |
D | GLU445 |
D | ARG446 |
D | GLY447 |
Functional Information from PROSITE/UniProt
site_id | PS00070 |
Number of Residues | 12 |
Details | ALDEHYDE_DEHYDR_CYS Aldehyde dehydrogenases cysteine active site. FsYSGQRCTAIK |
Chain | Residue | Details |
A | PHE286-LYS297 |
site_id | PS00687 |
Number of Residues | 8 |
Details | ALDEHYDE_DEHYDR_GLU Aldehyde dehydrogenases glutamic acid active site. LELGGKDP |
Chain | Residue | Details |
A | LEU258-PRO265 |