Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

7RAD

Crystal Structure Analysis of ALDH1B1

Functional Information from GO Data
ChainGOidnamespacecontents
A0004029molecular_functionaldehyde dehydrogenase (NAD+) activity
A0005654cellular_componentnucleoplasm
A0005739cellular_componentmitochondrion
A0005759cellular_componentmitochondrial matrix
A0005829cellular_componentcytosol
A0005975biological_processcarbohydrate metabolic process
A0006068biological_processethanol catabolic process
A0016491molecular_functionoxidoreductase activity
A0016620molecular_functionoxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor
A0043878molecular_functionglyceraldehyde-3-phosphate dehydrogenase (NAD+) (non-phosphorylating) activity
A0051287molecular_functionNAD binding
B0004029molecular_functionaldehyde dehydrogenase (NAD+) activity
B0005654cellular_componentnucleoplasm
B0005739cellular_componentmitochondrion
B0005759cellular_componentmitochondrial matrix
B0005829cellular_componentcytosol
B0005975biological_processcarbohydrate metabolic process
B0006068biological_processethanol catabolic process
B0016491molecular_functionoxidoreductase activity
B0016620molecular_functionoxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor
B0043878molecular_functionglyceraldehyde-3-phosphate dehydrogenase (NAD+) (non-phosphorylating) activity
B0051287molecular_functionNAD binding
Functional Information from PROSITE/UniProt
site_idPS00070
Number of Residues12
DetailsALDEHYDE_DEHYDR_CYS Aldehyde dehydrogenases cysteine active site. FfNMGQCCCAGS
ChainResidueDetails
APHE295-SER306

site_idPS00687
Number of Residues8
DetailsALDEHYDE_DEHYDR_GLU Aldehyde dehydrogenases glutamic acid active site. LELGGKSP
ChainResidueDetails
ALEU267-PRO274

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU10007, ECO:0000255|PROSITE-ProRule:PRU10008
ChainResidueDetails
AGLU268
BGLU268

site_idSWS_FT_FI2
Number of Residues2
DetailsACT_SITE: Nucleophile => ECO:0000255|PROSITE-ProRule:PRU10007, ECO:0000255|PROSITE-ProRule:PRU10008
ChainResidueDetails
ACYS302
BCYS302

site_idSWS_FT_FI3
Number of Residues2
DetailsBINDING: BINDING => ECO:0000250
ChainResidueDetails
AGLY245
BGLY245

site_idSWS_FT_FI4
Number of Residues2
DetailsSITE: Transition state stabilizer => ECO:0000250
ChainResidueDetails
AASN169
BASN169

site_idSWS_FT_FI5
Number of Residues4
DetailsMOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:Q9CZS1
ChainResidueDetails
ALYS34
ALYS412
BLYS34
BLYS412

site_idSWS_FT_FI6
Number of Residues12
DetailsMOD_RES: N6-succinyllysine; alternate => ECO:0000250|UniProtKB:Q9CZS1
ChainResidueDetails
ALYS35
BLYS382
BLYS397
BLYS409
ALYS347
ALYS366
ALYS382
ALYS397
ALYS409
BLYS35
BLYS347
BLYS366

site_idSWS_FT_FI7
Number of Residues2
DetailsMOD_RES: N6-succinyllysine => ECO:0000250|UniProtKB:Q9CZS1
ChainResidueDetails
ALYS64
BLYS64

220472

PDB entries from 2024-05-29

PDB statisticsPDBj update infoContact PDBjnumon