7RLU
Structure of ALDH1L1 (10-formyltetrahydrofolate dehydrogenase) in complex with NADP
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0003824 | molecular_function | catalytic activity |
A | 0004029 | molecular_function | aldehyde dehydrogenase (NAD+) activity |
A | 0004030 | molecular_function | aldehyde dehydrogenase [NAD(P)+] activity |
A | 0005737 | cellular_component | cytoplasm |
A | 0005829 | cellular_component | cytosol |
A | 0006730 | biological_process | one-carbon metabolic process |
A | 0006740 | biological_process | NADPH regeneration |
A | 0009058 | biological_process | biosynthetic process |
A | 0009258 | biological_process | 10-formyltetrahydrofolate catabolic process |
A | 0016155 | molecular_function | formyltetrahydrofolate 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 |
A | 0032991 | cellular_component | protein-containing complex |
A | 0033721 | molecular_function | aldehyde dehydrogenase (NADP+) activity |
A | 0038183 | biological_process | bile acid signaling pathway |
A | 0044877 | molecular_function | protein-containing complex binding |
A | 0046654 | biological_process | tetrahydrofolate biosynthetic process |
A | 0046655 | biological_process | folic acid metabolic process |
B | 0003824 | molecular_function | catalytic activity |
B | 0004029 | molecular_function | aldehyde dehydrogenase (NAD+) activity |
B | 0004030 | molecular_function | aldehyde dehydrogenase [NAD(P)+] activity |
B | 0005737 | cellular_component | cytoplasm |
B | 0005829 | cellular_component | cytosol |
B | 0006730 | biological_process | one-carbon metabolic process |
B | 0006740 | biological_process | NADPH regeneration |
B | 0009058 | biological_process | biosynthetic process |
B | 0009258 | biological_process | 10-formyltetrahydrofolate catabolic process |
B | 0016155 | molecular_function | formyltetrahydrofolate 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 |
B | 0032991 | cellular_component | protein-containing complex |
B | 0033721 | molecular_function | aldehyde dehydrogenase (NADP+) activity |
B | 0038183 | biological_process | bile acid signaling pathway |
B | 0044877 | molecular_function | protein-containing complex binding |
B | 0046654 | biological_process | tetrahydrofolate biosynthetic process |
B | 0046655 | biological_process | folic acid metabolic process |
C | 0003824 | molecular_function | catalytic activity |
C | 0004029 | molecular_function | aldehyde dehydrogenase (NAD+) activity |
C | 0004030 | molecular_function | aldehyde dehydrogenase [NAD(P)+] activity |
C | 0005737 | cellular_component | cytoplasm |
C | 0005829 | cellular_component | cytosol |
C | 0006730 | biological_process | one-carbon metabolic process |
C | 0006740 | biological_process | NADPH regeneration |
C | 0009058 | biological_process | biosynthetic process |
C | 0009258 | biological_process | 10-formyltetrahydrofolate catabolic process |
C | 0016155 | molecular_function | formyltetrahydrofolate 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 |
C | 0032991 | cellular_component | protein-containing complex |
C | 0033721 | molecular_function | aldehyde dehydrogenase (NADP+) activity |
C | 0038183 | biological_process | bile acid signaling pathway |
C | 0044877 | molecular_function | protein-containing complex binding |
C | 0046654 | biological_process | tetrahydrofolate biosynthetic process |
C | 0046655 | biological_process | folic acid metabolic process |
D | 0003824 | molecular_function | catalytic activity |
D | 0004029 | molecular_function | aldehyde dehydrogenase (NAD+) activity |
D | 0004030 | molecular_function | aldehyde dehydrogenase [NAD(P)+] activity |
D | 0005737 | cellular_component | cytoplasm |
D | 0005829 | cellular_component | cytosol |
D | 0006730 | biological_process | one-carbon metabolic process |
D | 0006740 | biological_process | NADPH regeneration |
D | 0009058 | biological_process | biosynthetic process |
D | 0009258 | biological_process | 10-formyltetrahydrofolate catabolic process |
D | 0016155 | molecular_function | formyltetrahydrofolate 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 |
D | 0032991 | cellular_component | protein-containing complex |
D | 0033721 | molecular_function | aldehyde dehydrogenase (NADP+) activity |
D | 0038183 | biological_process | bile acid signaling pathway |
D | 0044877 | molecular_function | protein-containing complex binding |
D | 0046654 | biological_process | tetrahydrofolate biosynthetic process |
D | 0046655 | biological_process | folic acid metabolic process |
Functional Information from PROSITE/UniProt
site_id | PS00070 |
Number of Residues | 12 |
Details | ALDEHYDE_DEHYDR_CYS Aldehyde dehydrogenases cysteine active site. FfNKGENCIAAG |
Chain | Residue | Details |
A | PHE700-GLY711 |
site_id | PS00373 |
Number of Residues | 24 |
Details | GART Phosphoribosylglycinamide formyltransferase active site. GfTIfWAdDgLDtGdlLlqkeceV |
Chain | Residue | Details |
A | GLY131-VAL154 |
site_id | PS00687 |
Number of Residues | 8 |
Details | ALDEHYDE_DEHYDR_GLU Aldehyde dehydrogenases glutamic acid active site. LELGGKSP |
Chain | Residue | Details |
A | LEU672-PRO679 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 4 |
Details | ACT_SITE: Proton donor => ECO:0000305|PubMed:10585460, ECO:0000305|PubMed:14729668 |
Chain | Residue | Details |
A | HIS106 | |
B | HIS106 | |
D | HIS106 | |
C | HIS106 |
site_id | SWS_FT_FI2 |
Number of Residues | 4 |
Details | ACT_SITE: Proton acceptor => ECO:0000305|PubMed:17302434 |
Chain | Residue | Details |
B | GLU673 | |
D | GLU673 | |
C | GLU673 | |
A | GLU673 |
site_id | SWS_FT_FI3 |
Number of Residues | 4 |
Details | ACT_SITE: Proton donor => ECO:0000305|PubMed:17302434, ECO:0000305|PubMed:21540484, ECO:0007744|PDB:2O2Q, ECO:0007744|PDB:3RHO |
Chain | Residue | Details |
B | CYS707 | |
D | CYS707 | |
C | CYS707 | |
A | CYS707 |
site_id | SWS_FT_FI4 |
Number of Residues | 8 |
Details | BINDING: BINDING => ECO:0000250|UniProtKB:O75891 |
Chain | Residue | Details |
B | GLN88 | |
D | GLN88 | |
D | ASP142 | |
C | GLN88 | |
C | ASP142 | |
A | ASP142 | |
B | ASP142 | |
A | GLN88 |
site_id | SWS_FT_FI5 |
Number of Residues | 16 |
Details | BINDING: BINDING => ECO:0000269|PubMed:17302434, ECO:0000269|PubMed:21540484, ECO:0007744|PDB:2O2Q, ECO:0007744|PDB:2O2R, ECO:0007744|PDB:3RHJ, ECO:0007744|PDB:3RHL, ECO:0007744|PDB:3RHO, ECO:0007744|PDB:3RHQ, ECO:0007744|PDB:3RHR |
Chain | Residue | Details |
A | GLY630 | |
B | ILE571 | |
B | LYS597 | |
B | GLY630 | |
B | GLY650 | |
D | ILE571 | |
D | LYS597 | |
D | GLY630 | |
D | GLY650 | |
C | ILE571 | |
C | LYS597 | |
C | GLY630 | |
C | GLY650 | |
A | LYS597 | |
A | GLY650 | |
A | ILE571 |
site_id | SWS_FT_FI6 |
Number of Residues | 8 |
Details | BINDING: BINDING => ECO:0000269|PubMed:17302434, ECO:0000269|PubMed:21540484, ECO:0007744|PDB:2O2Q, ECO:0007744|PDB:3RHJ, ECO:0007744|PDB:3RHL, ECO:0007744|PDB:3RHO, ECO:0007744|PDB:3RHQ, ECO:0007744|PDB:3RHR |
Chain | Residue | Details |
B | GLU673 | |
D | GLU673 | |
D | GLU804 | |
C | GLU673 | |
C | GLU804 | |
A | GLU804 | |
B | GLU804 | |
A | GLU673 |
site_id | SWS_FT_FI7 |
Number of Residues | 4 |
Details | BINDING: BINDING => ECO:0000269|PubMed:21540484, ECO:0007744|PDB:3RHO |
Chain | Residue | Details |
A | LYS757 | |
B | LYS757 | |
D | LYS757 | |
C | LYS757 |
site_id | SWS_FT_FI8 |
Number of Residues | 4 |
Details | SITE: Essential for catalytic activity => ECO:0000269|PubMed:10585460 |
Chain | Residue | Details |
A | ASP142 | |
B | ASP142 | |
D | ASP142 | |
C | ASP142 |
site_id | SWS_FT_FI9 |
Number of Residues | 16 |
Details | MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:O75891 |
Chain | Residue | Details |
D | SER9 | |
D | SER629 | |
D | SER631 | |
D | SER825 | |
C | SER9 | |
C | SER629 | |
C | SER631 | |
C | SER825 | |
A | SER9 | |
B | SER629 | |
B | SER631 | |
B | SER825 | |
A | SER629 | |
A | SER631 | |
A | SER825 | |
B | SER9 |
site_id | SWS_FT_FI10 |
Number of Residues | 8 |
Details | MOD_RES: N6-succinyllysine => ECO:0000250|UniProtKB:Q8R0Y6 |
Chain | Residue | Details |
D | LYS38 | |
D | LYS767 | |
C | LYS38 | |
C | LYS767 | |
A | LYS38 | |
A | LYS767 | |
B | LYS38 | |
B | LYS767 |
site_id | SWS_FT_FI11 |
Number of Residues | 4 |
Details | MOD_RES: O-(pantetheine 4'-phosphoryl)serine => ECO:0000255|PROSITE-ProRule:PRU00258, ECO:0000269|PubMed:17884809 |
Chain | Residue | Details |
A | SER354 | |
B | SER354 | |
D | SER354 | |
C | SER354 |
site_id | SWS_FT_FI12 |
Number of Residues | 4 |
Details | MOD_RES: N6-succinyllysine => ECO:0000250|UniProtKB:Q8K009 |
Chain | Residue | Details |
A | LYS660 | |
B | LYS660 | |
D | LYS660 | |
C | LYS660 |
site_id | SWS_FT_FI13 |
Number of Residues | 4 |
Details | MOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:Q3SY69 |
Chain | Residue | Details |
A | LYS882 | |
B | LYS882 | |
D | LYS882 | |
C | LYS882 |
Catalytic Information from CSA
site_id | MCSA1 |
Number of Residues | 3 |
Details | M-CSA 766 |
Chain | Residue | Details |
A | HIS106 | electrostatic stabiliser |
A | ASP142 | electrostatic stabiliser |
A | CYS707 |
site_id | MCSA2 |
Number of Residues | 3 |
Details | M-CSA 766 |
Chain | Residue | Details |
B | HIS106 | electrostatic stabiliser |
B | ASP142 | electrostatic stabiliser |
B | CYS707 |
site_id | MCSA3 |
Number of Residues | 3 |
Details | M-CSA 766 |
Chain | Residue | Details |
D | HIS106 | electrostatic stabiliser |
D | ASP142 | electrostatic stabiliser |
D | CYS707 |
site_id | MCSA4 |
Number of Residues | 3 |
Details | M-CSA 766 |
Chain | Residue | Details |
C | HIS106 | electrostatic stabiliser |
C | ASP142 | electrostatic stabiliser |
C | CYS707 |