3RHD
Crystal structure of glyceraldehyde-3-phosphate dehydrogenase GapN from Methanocaldococcus jannaschii DSM 2661 complexed with NADP
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0008911 | molecular_function | lactaldehyde dehydrogenase (NAD+) 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 | 0008911 | molecular_function | lactaldehyde dehydrogenase (NAD+) 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 | 0008911 | molecular_function | lactaldehyde dehydrogenase (NAD+) 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 | 0008911 | molecular_function | lactaldehyde dehydrogenase (NAD+) 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 | 21 |
Details | BINDING SITE FOR RESIDUE NAP A 500 |
Chain | Residue |
A | ILE137 |
A | GLY201 |
A | GLY205 |
A | ASP206 |
A | PHE219 |
A | SER222 |
A | VAL225 |
A | HOH550 |
A | HOH566 |
A | HOH576 |
A | HOH598 |
A | THR138 |
A | HOH600 |
A | HOH602 |
A | PHE140 |
A | HIS164 |
A | PRO165 |
A | SER166 |
A | SER167 |
A | LYS168 |
A | GLY199 |
site_id | AC2 |
Number of Residues | 19 |
Details | BINDING SITE FOR RESIDUE NAP B 500 |
Chain | Residue |
B | ILE137 |
B | THR138 |
B | PHE140 |
B | HIS164 |
B | PRO165 |
B | SER166 |
B | SER167 |
B | LYS168 |
B | GLY199 |
B | GLY201 |
B | GLY205 |
B | ASP206 |
B | PHE219 |
B | SER222 |
B | VAL225 |
B | HOH562 |
B | HOH586 |
B | HOH660 |
B | HOH813 |
site_id | AC3 |
Number of Residues | 17 |
Details | BINDING SITE FOR RESIDUE NAP C 500 |
Chain | Residue |
C | ILE137 |
C | THR138 |
C | PHE140 |
C | HIS164 |
C | SER166 |
C | SER167 |
C | LYS168 |
C | GLY199 |
C | GLY201 |
C | GLY205 |
C | ASP206 |
C | PHE219 |
C | SER222 |
C | VAL225 |
C | HOH537 |
C | HOH588 |
C | HOH753 |
site_id | AC4 |
Number of Residues | 21 |
Details | BINDING SITE FOR RESIDUE NAP D 500 |
Chain | Residue |
D | ILE137 |
D | THR138 |
D | PHE140 |
D | HIS164 |
D | PRO165 |
D | SER166 |
D | SER167 |
D | LYS168 |
D | GLY199 |
D | GLY201 |
D | GLU202 |
D | GLY205 |
D | ASP206 |
D | PHE219 |
D | SER222 |
D | VAL225 |
D | HOH530 |
D | HOH537 |
D | HOH544 |
D | HOH553 |
D | HOH794 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 8 |
Details | ACT_SITE: ACT_SITE => ECO:0000250 |
Chain | Residue | Details |
A | GLU241 | |
A | CYS275 | |
B | GLU241 | |
B | CYS275 | |
C | GLU241 | |
C | CYS275 | |
D | GLU241 | |
D | CYS275 |
site_id | SWS_FT_FI2 |
Number of Residues | 4 |
Details | BINDING: BINDING => ECO:0000250 |
Chain | Residue | Details |
A | GLY221 | |
B | GLY221 | |
C | GLY221 | |
D | GLY221 |