1LUA
Structure of methylene-tetrahydromethanopterin dehydrogenase from Methylobacterium extorquens AM1 complexed with NADP
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0004488 | molecular_function | methylenetetrahydrofolate dehydrogenase (NADP+) activity |
A | 0005737 | cellular_component | cytoplasm |
A | 0006730 | biological_process | one-carbon metabolic process |
A | 0016491 | molecular_function | oxidoreductase activity |
A | 0046294 | biological_process | formaldehyde catabolic process |
B | 0004488 | molecular_function | methylenetetrahydrofolate dehydrogenase (NADP+) activity |
B | 0005737 | cellular_component | cytoplasm |
B | 0006730 | biological_process | one-carbon metabolic process |
B | 0016491 | molecular_function | oxidoreductase activity |
B | 0046294 | biological_process | formaldehyde catabolic process |
C | 0004488 | molecular_function | methylenetetrahydrofolate dehydrogenase (NADP+) activity |
C | 0005737 | cellular_component | cytoplasm |
C | 0006730 | biological_process | one-carbon metabolic process |
C | 0016491 | molecular_function | oxidoreductase activity |
C | 0046294 | biological_process | formaldehyde catabolic process |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 28 |
Details | BINDING SITE FOR RESIDUE NAP A 456 |
Chain | Residue |
A | ASN97 |
A | LYS156 |
A | ALA196 |
A | GLY197 |
A | ALA198 |
A | ILE199 |
A | LEU201 |
A | TYR221 |
A | ASN222 |
A | LYS256 |
A | HOH3270 |
A | THR102 |
A | HOH3395 |
A | HOH3456 |
A | HOH3474 |
A | HOH3515 |
A | HOH3644 |
A | HOH3687 |
A | HOH3813 |
A | HOH3875 |
A | HOH3893 |
A | ALA127 |
A | THR129 |
A | GLY130 |
A | PRO131 |
A | VAL132 |
A | GLY151 |
A | ARG152 |
site_id | AC2 |
Number of Residues | 23 |
Details | BINDING SITE FOR RESIDUE NAP B 1456 |
Chain | Residue |
B | ASN97 |
B | THR102 |
B | THR129 |
B | GLY130 |
B | PRO131 |
B | VAL132 |
B | GLY151 |
B | ARG152 |
B | LYS156 |
B | ALA196 |
B | GLY197 |
B | ALA198 |
B | ILE199 |
B | LEU201 |
B | TYR221 |
B | ASN222 |
B | LYS256 |
B | HOH3352 |
B | HOH3537 |
B | HOH3579 |
B | HOH3684 |
B | HOH3696 |
B | HOH3896 |
site_id | AC3 |
Number of Residues | 29 |
Details | BINDING SITE FOR RESIDUE NAP C 2456 |
Chain | Residue |
C | ASN97 |
C | THR102 |
C | ALA127 |
C | THR129 |
C | GLY130 |
C | PRO131 |
C | VAL132 |
C | GLY151 |
C | ARG152 |
C | LYS156 |
C | ALA196 |
C | GLY197 |
C | ALA198 |
C | ILE199 |
C | LEU201 |
C | TYR221 |
C | ASN222 |
C | LYS256 |
C | HOH3243 |
C | HOH3433 |
C | HOH3445 |
C | HOH3603 |
C | HOH3646 |
C | HOH3709 |
C | HOH3731 |
C | HOH3764 |
C | HOH3766 |
C | HOH3842 |
C | HOH3855 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 12 |
Details | BINDING: BINDING => ECO:0000269|PubMed:11297742 |
Chain | Residue | Details |
A | GLY130 | |
C | LYS153 | |
C | ALA196 | |
C | LEU257 | |
A | LYS153 | |
A | ALA196 | |
A | LEU257 | |
B | GLY130 | |
B | LYS153 | |
B | ALA196 | |
B | LEU257 | |
C | GLY130 |