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7S7G

Crystal Structure Analysis of Human VLCAD

Functional Information from GO Data
ChainGOidnamespacecontents
A0000062molecular_functionfatty-acyl-CoA binding
A0001659biological_processtemperature homeostasis
A0003995molecular_functionacyl-CoA dehydrogenase activity
A0004466molecular_functionlong-chain fatty acyl-CoA dehydrogenase activity
A0005515molecular_functionprotein binding
A0005739cellular_componentmitochondrion
A0005743cellular_componentmitochondrial inner membrane
A0005759cellular_componentmitochondrial matrix
A0006629biological_processlipid metabolic process
A0006631biological_processfatty acid metabolic process
A0006635biological_processfatty acid beta-oxidation
A0015980biological_processenergy derivation by oxidation of organic compounds
A0016491molecular_functionoxidoreductase activity
A0016627molecular_functionoxidoreductase activity, acting on the CH-CH group of donors
A0017099molecular_functionvery-long-chain fatty acyl-CoA dehydrogenase activity
A0030855biological_processepithelial cell differentiation
A0031966cellular_componentmitochondrial membrane
A0033539biological_processfatty acid beta-oxidation using acyl-CoA dehydrogenase
A0042645cellular_componentmitochondrial nucleoid
A0042802molecular_functionidentical protein binding
A0045717biological_processnegative regulation of fatty acid biosynthetic process
A0046322biological_processnegative regulation of fatty acid oxidation
A0050660molecular_functionflavin adenine dinucleotide binding
A0090181biological_processregulation of cholesterol metabolic process
Functional Information from PROSITE/UniProt
site_idPS00072
Number of Residues13
DetailsACYL_COA_DH_1 Acyl-CoA dehydrogenases signature 1. CLTEpsSGSDaaS
ChainResidueDetails
ACYS175-SER187

site_idPS00073
Number of Residues20
DetailsACYL_COA_DH_2 Acyl-CoA dehydrogenases signature 2. QiMGGmGFmkEpgveRvlrD
ChainResidueDetails
AGLN395-ASP414

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsActive site: {"description":"Proton acceptor","evidences":[{"source":"PubMed","id":"18227065","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9461620","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2UXW","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3B96","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues16
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"18227065","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2UXW","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3B96","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues7
DetailsModified residue: {"description":"N6-succinyllysine; alternate","evidences":[{"source":"UniProtKB","id":"P50544","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues3
DetailsModified residue: {"description":"N6-succinyllysine","evidences":[{"source":"UniProtKB","id":"P50544","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues1
DetailsModified residue: {"description":"S-nitrosocysteine","evidences":[{"source":"UniProtKB","id":"P50544","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues2
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"P50544","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues2
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

249524

PDB entries from 2026-02-18

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