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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
A0005654cellular_componentnucleoplasm
A0005730cellular_componentnucleolus
A0005739cellular_componentmitochondrion
A0005743cellular_componentmitochondrial inner membrane
A0005759cellular_componentmitochondrial matrix
A0006631biological_processfatty acid metabolic process
A0009062biological_processfatty acid catabolic process
A0009409biological_processresponse to cold
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
DetailsACT_SITE: Proton acceptor => ECO:0000269|PubMed:18227065, ECO:0000269|PubMed:9461620, ECO:0007744|PDB:2UXW, ECO:0007744|PDB:3B96
ChainResidueDetails
AGLU422

site_idSWS_FT_FI2
Number of Residues5
DetailsBINDING: BINDING => ECO:0000269|PubMed:18227065, ECO:0007744|PDB:2UXW, ECO:0007744|PDB:3B96
ChainResidueDetails
APHE174
ATRP209
APHE421
ATHR424
AGLN522

site_idSWS_FT_FI3
Number of Residues7
DetailsMOD_RES: N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P50544
ChainResidueDetails
ALYS31
ALYS199
ALYS236
ALYS238
ALYS291
ALYS442
ALYS516

site_idSWS_FT_FI4
Number of Residues3
DetailsMOD_RES: N6-succinyllysine => ECO:0000250|UniProtKB:P50544
ChainResidueDetails
ALYS155
ALYS332
ALYS599

site_idSWS_FT_FI5
Number of Residues1
DetailsMOD_RES: S-nitrosocysteine => ECO:0000250|UniProtKB:P50544
ChainResidueDetails
ACYS197

site_idSWS_FT_FI6
Number of Residues2
DetailsMOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:P50544
ChainResidueDetails
ALYS258
ALYS510

site_idSWS_FT_FI7
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:23186163
ChainResidueDetails
ASER477
ASER482

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PDB entries from 2024-06-12

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