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

1SO8

Abeta-bound human ABAD structure [also known as 3-hydroxyacyl-CoA dehydrogenase type II (Type II HADH), Endoplasmic reticulum-associated amyloid beta-peptide binding protein (ERAB)]

Functional Information from GO Data
ChainGOidnamespacecontents
A0000049molecular_functiontRNA binding
A0003723molecular_functionRNA binding
A0003857molecular_function3-hydroxyacyl-CoA dehydrogenase activity
A0004303molecular_functionestradiol 17-beta-dehydrogenase [NAD(P)+] activity
A0005515molecular_functionprotein binding
A0005737cellular_componentcytoplasm
A0005739cellular_componentmitochondrion
A0005759cellular_componentmitochondrial matrix
A0005886cellular_componentplasma membrane
A0006550biological_processisoleucine catabolic process
A0006629biological_processlipid metabolic process
A0006631biological_processfatty acid metabolic process
A0006635biological_processfatty acid beta-oxidation
A0006699biological_processbile acid biosynthetic process
A0007005biological_processmitochondrion organization
A0008033biological_processtRNA processing
A0008202biological_processsteroid metabolic process
A0008207biological_processC21-steroid hormone metabolic process
A0008209biological_processandrogen metabolic process
A0008210biological_processestrogen metabolic process
A0008709molecular_functioncholate 7-alpha-dehydrogenase activity
A0016491molecular_functionoxidoreductase activity
A0030283molecular_functiontestosterone dehydrogenase [NAD(P)+] activity
A0030678cellular_componentmitochondrial ribonuclease P complex
A0042645cellular_componentmitochondrial nucleoid
A0043527cellular_componenttRNA methyltransferase complex
A0044594molecular_function17-beta-hydroxysteroid dehydrogenase (NAD+) activity
A0047015molecular_function3-hydroxy-2-methylbutyryl-CoA dehydrogenase activity
A0047035molecular_functiontestosterone dehydrogenase (NAD+) activity
A0047044molecular_functionandrostan-3-alpha,17-beta-diol dehydrogenase activity
A0051289biological_processprotein homotetramerization
A0062173biological_processbrexanolone metabolic process
A0070901biological_processmitochondrial tRNA methylation
A0097745biological_processmitochondrial tRNA 5'-end processing
A0106281molecular_functionchenodeoxycholate 7-alpha-dehydrogenase (NAD+) activity
A0106282molecular_functionisoursodeoxycholate 7-beta-dehydrogenase (NAD+) activity
A0106283molecular_functionursodeoxycholate 7-beta-dehydrogenase (NAD+) activity
A1990180biological_processmitochondrial tRNA 3'-end processing
Functional Information from PDB Data
site_idAC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE NA A 301
ChainResidue
ASER67
ASER67
AGLU68
AGLU68
ALYS69
ALYS69

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE NA A 302
ChainResidue
AHOH545
AHOH560
AHOH602
AGLY17
ASER20
AHOH522

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CL A 303
ChainResidue
AALA154
ASER155
AGLY173
AILE175
AVAL176
AHOH570

Functional Information from PROSITE/UniProt
site_idPS00061
Number of Residues29
DetailsADH_SHORT Short-chain dehydrogenases/reductases family signature. SvaafegqvgQaaYSASKGGIvGMTlPIA
ChainResidueDetails
ASER155-ALA183

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Proton acceptor => ECO:0000269|PubMed:15087549
ChainResidueDetails
ATYR168

site_idSWS_FT_FI2
Number of Residues10
DetailsBINDING: BINDING => ECO:0000269|PubMed:15342248, ECO:0007744|PDB:1U7T
ChainResidueDetails
ASER20
ATHR203
ALEU22
AASP41
AASP64
AVAL65
ACYS91
ATYR168
ALYS172
APHE201

site_idSWS_FT_FI3
Number of Residues1
DetailsBINDING: BINDING => ECO:0000269|PubMed:15087549
ChainResidueDetails
ASER155

site_idSWS_FT_FI4
Number of Residues1
DetailsMOD_RES: N-acetylalanine => ECO:0007744|PubMed:25944712
ChainResidueDetails
AALA2

site_idSWS_FT_FI5
Number of Residues2
DetailsMOD_RES: N6-succinyllysine; alternate => ECO:0000250|UniProtKB:O08756
ChainResidueDetails
ALYS53
ALYS212

site_idSWS_FT_FI6
Number of Residues3
DetailsMOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:O08756
ChainResidueDetails
ALYS69
ALYS99
ALYS105

Catalytic Information from CSA
site_idCSA1
Number of Residues4
DetailsAnnotated By Reference To The Literature 1ybv
ChainResidueDetails
ALYS172
ASER155
AASN121
ATYR168

site_idCSA2
Number of Residues2
DetailsAnnotated By Reference To The Literature 1ybv
ChainResidueDetails
ALYS172
AGLN165

site_idCSA3
Number of Residues2
DetailsAnnotated By Reference To The Literature 1ybv
ChainResidueDetails
ALYS172
ATYR168

222926

PDB entries from 2024-07-24

PDB statisticsPDBj update infoContact PDBjnumon