7RLT
Structure of ligand-free ALDH1L1 (10-formyltetrahydrofolate dehydrogenase)
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 | 0035999 | biological_process | tetrahydrofolate interconversion |
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 | 0035999 | biological_process | tetrahydrofolate interconversion |
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 | 0035999 | biological_process | tetrahydrofolate interconversion |
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 | 0035999 | biological_process | tetrahydrofolate interconversion |
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 | 308 |
Details | Domain: {"description":"Carrier","evidences":[{"source":"PROSITE-ProRule","id":"PRU00258","evidenceCode":"ECO:0000255"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI2 |
Number of Residues | 1940 |
Details | Region: {"description":"Aldehyde dehydrogenase domain","evidences":[{"source":"PubMed","id":"10585460","evidenceCode":"ECO:0000305"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI3 |
Number of Residues | 4 |
Details | Active site: {"description":"Proton acceptor","evidences":[{"source":"PubMed","id":"17302434","evidenceCode":"ECO:0000305"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI4 |
Number of Residues | 4 |
Details | Active site: {"description":"Proton donor","evidences":[{"source":"PubMed","id":"17302434","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"21540484","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"2O2Q","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3RHO","evidenceCode":"ECO:0007744"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI5 |
Number of Residues | 44 |
Details | Binding site: {"evidences":[{"source":"PubMed","id":"17302434","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"21540484","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2O2Q","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2O2R","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3RHJ","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3RHL","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3RHO","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3RHQ","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3RHR","evidenceCode":"ECO:0007744"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI6 |
Number of Residues | 12 |
Details | Binding site: {"evidences":[{"source":"PubMed","id":"17302434","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"21540484","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2O2Q","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3RHJ","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3RHL","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3RHO","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3RHQ","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3RHR","evidenceCode":"ECO:0007744"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI7 |
Number of Residues | 4 |
Details | Binding site: {"evidences":[{"source":"PubMed","id":"21540484","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3RHO","evidenceCode":"ECO:0007744"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI8 |
Number of Residues | 4 |
Details | Modified residue: {"description":"O-(pantetheine 4'-phosphoryl)serine","evidences":[{"source":"PROSITE-ProRule","id":"PRU00258","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"17884809","evidenceCode":"ECO:0000269"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI9 |
Number of Residues | 12 |
Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"O75891","evidenceCode":"ECO:0000250"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI10 |
Number of Residues | 4 |
Details | Modified residue: {"description":"N6-succinyllysine","evidences":[{"source":"UniProtKB","id":"Q8K009","evidenceCode":"ECO:0000250"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI11 |
Number of Residues | 4 |
Details | Modified residue: {"description":"N6-succinyllysine","evidences":[{"source":"UniProtKB","id":"Q8R0Y6","evidenceCode":"ECO:0000250"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI12 |
Number of Residues | 4 |
Details | Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"Q3SY69","evidenceCode":"ECO:0000250"}]} |
Chain | Residue | Details |
Catalytic Information from CSA