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7RLT

Structure of ligand-free ALDH1L1 (10-formyltetrahydrofolate dehydrogenase)

Functional Information from GO Data
ChainGOidnamespacecontents
A0003824molecular_functioncatalytic activity
A0004029molecular_functionaldehyde dehydrogenase (NAD+) activity
A0004030molecular_functionaldehyde dehydrogenase [NAD(P)+] activity
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0006730biological_processone-carbon metabolic process
A0006740biological_processNADPH regeneration
A0009058biological_processbiosynthetic process
A0009258biological_process10-formyltetrahydrofolate catabolic process
A0016155molecular_functionformyltetrahydrofolate dehydrogenase activity
A0016491molecular_functionoxidoreductase activity
A0016620molecular_functionoxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor
A0032991cellular_componentprotein-containing complex
A0033721molecular_functionaldehyde dehydrogenase (NADP+) activity
A0035999biological_processtetrahydrofolate interconversion
A0044877molecular_functionprotein-containing complex binding
A0046654biological_processtetrahydrofolate biosynthetic process
A0046655biological_processfolic acid metabolic process
B0003824molecular_functioncatalytic activity
B0004029molecular_functionaldehyde dehydrogenase (NAD+) activity
B0004030molecular_functionaldehyde dehydrogenase [NAD(P)+] activity
B0005737cellular_componentcytoplasm
B0005829cellular_componentcytosol
B0006730biological_processone-carbon metabolic process
B0006740biological_processNADPH regeneration
B0009058biological_processbiosynthetic process
B0009258biological_process10-formyltetrahydrofolate catabolic process
B0016155molecular_functionformyltetrahydrofolate dehydrogenase activity
B0016491molecular_functionoxidoreductase activity
B0016620molecular_functionoxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor
B0032991cellular_componentprotein-containing complex
B0033721molecular_functionaldehyde dehydrogenase (NADP+) activity
B0035999biological_processtetrahydrofolate interconversion
B0044877molecular_functionprotein-containing complex binding
B0046654biological_processtetrahydrofolate biosynthetic process
B0046655biological_processfolic acid metabolic process
C0003824molecular_functioncatalytic activity
C0004029molecular_functionaldehyde dehydrogenase (NAD+) activity
C0004030molecular_functionaldehyde dehydrogenase [NAD(P)+] activity
C0005737cellular_componentcytoplasm
C0005829cellular_componentcytosol
C0006730biological_processone-carbon metabolic process
C0006740biological_processNADPH regeneration
C0009058biological_processbiosynthetic process
C0009258biological_process10-formyltetrahydrofolate catabolic process
C0016155molecular_functionformyltetrahydrofolate dehydrogenase activity
C0016491molecular_functionoxidoreductase activity
C0016620molecular_functionoxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor
C0032991cellular_componentprotein-containing complex
C0033721molecular_functionaldehyde dehydrogenase (NADP+) activity
C0035999biological_processtetrahydrofolate interconversion
C0044877molecular_functionprotein-containing complex binding
C0046654biological_processtetrahydrofolate biosynthetic process
C0046655biological_processfolic acid metabolic process
D0003824molecular_functioncatalytic activity
D0004029molecular_functionaldehyde dehydrogenase (NAD+) activity
D0004030molecular_functionaldehyde dehydrogenase [NAD(P)+] activity
D0005737cellular_componentcytoplasm
D0005829cellular_componentcytosol
D0006730biological_processone-carbon metabolic process
D0006740biological_processNADPH regeneration
D0009058biological_processbiosynthetic process
D0009258biological_process10-formyltetrahydrofolate catabolic process
D0016155molecular_functionformyltetrahydrofolate dehydrogenase activity
D0016491molecular_functionoxidoreductase activity
D0016620molecular_functionoxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor
D0032991cellular_componentprotein-containing complex
D0033721molecular_functionaldehyde dehydrogenase (NADP+) activity
D0035999biological_processtetrahydrofolate interconversion
D0044877molecular_functionprotein-containing complex binding
D0046654biological_processtetrahydrofolate biosynthetic process
D0046655biological_processfolic acid metabolic process
Functional Information from PROSITE/UniProt
site_idPS00070
Number of Residues12
DetailsALDEHYDE_DEHYDR_CYS Aldehyde dehydrogenases cysteine active site. FfNKGENCIAAG
ChainResidueDetails
APHE700-GLY711

site_idPS00373
Number of Residues24
DetailsGART Phosphoribosylglycinamide formyltransferase active site. GfTIfWAdDgLDtGdlLlqkeceV
ChainResidueDetails
AGLY131-VAL154

site_idPS00687
Number of Residues8
DetailsALDEHYDE_DEHYDR_GLU Aldehyde dehydrogenases glutamic acid active site. LELGGKSP
ChainResidueDetails
ALEU672-PRO679

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues308
DetailsDomain: {"description":"Carrier","evidences":[{"source":"PROSITE-ProRule","id":"PRU00258","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues1940
DetailsRegion: {"description":"Aldehyde dehydrogenase domain","evidences":[{"source":"PubMed","id":"10585460","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues4
DetailsActive site: {"description":"Proton acceptor","evidences":[{"source":"PubMed","id":"17302434","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues4
DetailsActive 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"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues44
DetailsBinding 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"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues12
DetailsBinding 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"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues4
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"21540484","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3RHO","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI8
Number of Residues4
DetailsModified residue: {"description":"O-(pantetheine 4'-phosphoryl)serine","evidences":[{"source":"PROSITE-ProRule","id":"PRU00258","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"17884809","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI9
Number of Residues12
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"O75891","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI10
Number of Residues4
DetailsModified residue: {"description":"N6-succinyllysine","evidences":[{"source":"UniProtKB","id":"Q8K009","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI11
Number of Residues4
DetailsModified residue: {"description":"N6-succinyllysine","evidences":[{"source":"UniProtKB","id":"Q8R0Y6","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI12
Number of Residues4
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"Q3SY69","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idMCSA1
Number of Residues1
DetailsM-CSA 766
ChainResidueDetails
ACYS707

site_idMCSA2
Number of Residues1
DetailsM-CSA 766
ChainResidueDetails
BCYS707

site_idMCSA3
Number of Residues1
DetailsM-CSA 766
ChainResidueDetails
CCYS707

site_idMCSA4
Number of Residues1
DetailsM-CSA 766
ChainResidueDetails
DCYS707

239803

PDB entries from 2025-08-06

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