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4I8Q

Structure of the aminoaldehyde dehydrogenase 1 E260A mutant from Solanum lycopersicum (SlAMADH1-E260A)

Functional Information from GO Data
ChainGOidnamespacecontents
A0008802molecular_functionbetaine-aldehyde dehydrogenase (NAD+) activity
A0016491molecular_functionoxidoreductase activity
A0019145molecular_functionaminobutyraldehyde dehydrogenase (NAD+) activity
A0019285biological_processglycine betaine biosynthetic process from choline
A0031402molecular_functionsodium ion binding
A0042803molecular_functionprotein homodimerization activity
A0047105molecular_function4-trimethylammoniobutyraldehyde dehydrogenase activity
A0047107molecular_functiongamma-guanidinobutyraldehyde dehydrogenase (NAD+) activity
A0110095biological_processcellular detoxification of aldehyde
Functional Information from PDB Data
site_idAC1
Number of Residues25
DetailsBINDING SITE FOR RESIDUE NAD A 601
ChainResidue
AILE158
AGLY218
AGLY222
AGLY223
APHE236
ATHR237
AGLY238
ASER239
ATHR242
AILE246
AALA260
ATHR159
ALEU261
AGLY262
ACYS295
AGLU394
APHE396
ATRP460
APRO160
ATRP161
AASN162
ALYS185
APRO186
ASER187
AGLU188

site_idAC2
Number of Residues3
DetailsBINDING SITE FOR RESIDUE EDO A 602
ChainResidue
ATHR35
AGLU37
ALYS372

site_idAC3
Number of Residues2
DetailsBINDING SITE FOR RESIDUE EDO A 603
ChainResidue
AILE324
AHIS369

site_idAC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE EDO A 605
ChainResidue
AASN26
AILE38
AILE39
AGLY40

site_idAC5
Number of Residues1
DetailsBINDING SITE FOR RESIDUE PEG A 607
ChainResidue
AGLU493

site_idAC6
Number of Residues1
DetailsBINDING SITE FOR RESIDUE EDO A 608
ChainResidue
APRO241

site_idAC7
Number of Residues3
DetailsBINDING SITE FOR RESIDUE EDO A 609
ChainResidue
AASP113
ATRP170
AASN456

site_idAC8
Number of Residues3
DetailsBINDING SITE FOR RESIDUE NA A 612
ChainResidue
AILE31
AASP99
ALEU189

Functional Information from PROSITE/UniProt
site_idPS00070
Number of Residues12
DetailsALDEHYDE_DEHYDR_CYS Aldehyde dehydrogenases cysteine active site. FaNTGQVCSATS
ChainResidueDetails
APHE288-SER299

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsActive site: {"description":"Proton acceptor","evidences":[{"source":"PROSITE-ProRule","id":"PRU10007","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"23408433","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues1
DetailsActive site: {"description":"Nucleophile","evidences":[{"source":"PROSITE-ProRule","id":"PRU10008","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"23408433","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues12
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"23408433","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4I8Q","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4I9B","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues3
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"23408433","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4I8Q","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues1
DetailsSite: {"description":"Transition state stabilizer","evidences":[{"source":"UniProtKB","id":"P20000","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

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PDB entries from 2026-04-01

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