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8PHF

Cryo-EM structure of human ACAD9-S191A

Functional Information from GO Data
ChainGOidnamespacecontents
A0001676biological_processlong-chain fatty acid metabolic process
A0003995molecular_functionacyl-CoA dehydrogenase activity
A0004466molecular_functionlong-chain fatty acyl-CoA dehydrogenase activity
A0005515molecular_functionprotein binding
A0005634cellular_componentnucleus
A0005739cellular_componentmitochondrion
A0005743cellular_componentmitochondrial inner membrane
A0006631biological_processfatty acid metabolic process
A0016020cellular_componentmembrane
A0016491molecular_functionoxidoreductase activity
A0016627molecular_functionoxidoreductase activity, acting on the CH-CH group of donors
A0030425cellular_componentdendrite
A0031966cellular_componentmitochondrial membrane
A0032981biological_processmitochondrial respiratory chain complex I assembly
A0050660molecular_functionflavin adenine dinucleotide binding
A0051791biological_processmedium-chain fatty acid metabolic process
A0070991molecular_functionmedium-chain fatty acyl-CoA dehydrogenase activity
B0001676biological_processlong-chain fatty acid metabolic process
B0003995molecular_functionacyl-CoA dehydrogenase activity
B0004466molecular_functionlong-chain fatty acyl-CoA dehydrogenase activity
B0005515molecular_functionprotein binding
B0005634cellular_componentnucleus
B0005739cellular_componentmitochondrion
B0005743cellular_componentmitochondrial inner membrane
B0006631biological_processfatty acid metabolic process
B0016020cellular_componentmembrane
B0016491molecular_functionoxidoreductase activity
B0016627molecular_functionoxidoreductase activity, acting on the CH-CH group of donors
B0030425cellular_componentdendrite
B0031966cellular_componentmitochondrial membrane
B0032981biological_processmitochondrial respiratory chain complex I assembly
B0050660molecular_functionflavin adenine dinucleotide binding
B0051791biological_processmedium-chain fatty acid metabolic process
B0070991molecular_functionmedium-chain fatty acyl-CoA dehydrogenase activity
Functional Information from PROSITE/UniProt
site_idPS00072
Number of Residues13
DetailsACYL_COA_DH_1 Acyl-CoA dehydrogenases signature 1. CLTEpaSGSDaaA
ChainResidueDetails
ACYS179-ALA191

site_idPS00073
Number of Residues20
DetailsACYL_COA_DH_2 Acyl-CoA dehydrogenases signature 2. QiLGGlGYtrDypyeRilrD
ChainResidueDetails
AGLN399-ASP418

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Proton acceptor => ECO:0000305|PubMed:24158852
ChainResidueDetails
AGLU426
BGLU426

site_idSWS_FT_FI2
Number of Residues2
DetailsMOD_RES: N6-acetyllysine => ECO:0007744|PubMed:19608861
ChainResidueDetails
ALYS41
BLYS41

site_idSWS_FT_FI3
Number of Residues2
DetailsMOD_RES: N6-succinyllysine => ECO:0000250|UniProtKB:Q8JZN5
ChainResidueDetails
ALYS92
BLYS92

site_idSWS_FT_FI4
Number of Residues2
DetailsMOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:Q8JZN5
ChainResidueDetails
ATHR478
BTHR478

site_idSWS_FT_FI5
Number of Residues2
DetailsMOD_RES: N6-succinyllysine; alternate => ECO:0000250|UniProtKB:Q8JZN5
ChainResidueDetails
ALYS521
BLYS521

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PDB entries from 2025-06-18

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