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7RLU

Structure of ALDH1L1 (10-formyltetrahydrofolate dehydrogenase) in complex with NADP

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
A0038183biological_processbile acid signaling pathway
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
B0038183biological_processbile acid signaling pathway
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
C0038183biological_processbile acid signaling pathway
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
D0038183biological_processbile acid signaling pathway
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 Residues4
DetailsACT_SITE: Proton donor => ECO:0000305|PubMed:10585460, ECO:0000305|PubMed:14729668
ChainResidueDetails
AHIS106
BHIS106
DHIS106
CHIS106

site_idSWS_FT_FI2
Number of Residues4
DetailsACT_SITE: Proton acceptor => ECO:0000305|PubMed:17302434
ChainResidueDetails
BGLU673
DGLU673
CGLU673
AGLU673

site_idSWS_FT_FI3
Number of Residues4
DetailsACT_SITE: Proton donor => ECO:0000305|PubMed:17302434, ECO:0000305|PubMed:21540484, ECO:0007744|PDB:2O2Q, ECO:0007744|PDB:3RHO
ChainResidueDetails
BCYS707
DCYS707
CCYS707
ACYS707

site_idSWS_FT_FI4
Number of Residues8
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:O75891
ChainResidueDetails
BGLN88
DGLN88
DASP142
CGLN88
CASP142
AASP142
BASP142
AGLN88

site_idSWS_FT_FI5
Number of Residues16
DetailsBINDING: 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
ChainResidueDetails
AGLY630
BILE571
BLYS597
BGLY630
BGLY650
DILE571
DLYS597
DGLY630
DGLY650
CILE571
CLYS597
CGLY630
CGLY650
ALYS597
AGLY650
AILE571

site_idSWS_FT_FI6
Number of Residues8
DetailsBINDING: 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
ChainResidueDetails
BGLU673
DGLU673
DGLU804
CGLU673
CGLU804
AGLU804
BGLU804
AGLU673

site_idSWS_FT_FI7
Number of Residues4
DetailsBINDING: BINDING => ECO:0000269|PubMed:21540484, ECO:0007744|PDB:3RHO
ChainResidueDetails
ALYS757
BLYS757
DLYS757
CLYS757

site_idSWS_FT_FI8
Number of Residues4
DetailsSITE: Essential for catalytic activity => ECO:0000269|PubMed:10585460
ChainResidueDetails
AASP142
BASP142
DASP142
CASP142

site_idSWS_FT_FI9
Number of Residues16
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:O75891
ChainResidueDetails
DSER9
DSER629
DSER631
DSER825
CSER9
CSER629
CSER631
CSER825
ASER9
BSER629
BSER631
BSER825
ASER629
ASER631
ASER825
BSER9

site_idSWS_FT_FI10
Number of Residues8
DetailsMOD_RES: N6-succinyllysine => ECO:0000250|UniProtKB:Q8R0Y6
ChainResidueDetails
DLYS38
DLYS767
CLYS38
CLYS767
ALYS38
ALYS767
BLYS38
BLYS767

site_idSWS_FT_FI11
Number of Residues4
DetailsMOD_RES: O-(pantetheine 4'-phosphoryl)serine => ECO:0000255|PROSITE-ProRule:PRU00258, ECO:0000269|PubMed:17884809
ChainResidueDetails
ASER354
BSER354
DSER354
CSER354

site_idSWS_FT_FI12
Number of Residues4
DetailsMOD_RES: N6-succinyllysine => ECO:0000250|UniProtKB:Q8K009
ChainResidueDetails
ALYS660
BLYS660
DLYS660
CLYS660

site_idSWS_FT_FI13
Number of Residues4
DetailsMOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:Q3SY69
ChainResidueDetails
ALYS882
BLYS882
DLYS882
CLYS882

Catalytic Information from CSA
site_idMCSA1
Number of Residues3
DetailsM-CSA 766
ChainResidueDetails
AHIS106electrostatic stabiliser
AASP142electrostatic stabiliser
ACYS707

site_idMCSA2
Number of Residues3
DetailsM-CSA 766
ChainResidueDetails
BHIS106electrostatic stabiliser
BASP142electrostatic stabiliser
BCYS707

site_idMCSA3
Number of Residues3
DetailsM-CSA 766
ChainResidueDetails
DHIS106electrostatic stabiliser
DASP142electrostatic stabiliser
DCYS707

site_idMCSA4
Number of Residues3
DetailsM-CSA 766
ChainResidueDetails
CHIS106electrostatic stabiliser
CASP142electrostatic stabiliser
CCYS707

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PDB entries from 2024-06-12

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