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3B7W

Crystal structure of human acyl-CoA synthetase medium-chain family member 2A, with L64P mutation

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0004321molecular_functionfatty-acyl-CoA synthase activity
A0005524molecular_functionATP binding
A0005739cellular_componentmitochondrion
A0005759cellular_componentmitochondrial matrix
A0006629biological_processlipid metabolic process
A0006631biological_processfatty acid metabolic process
A0006633biological_processfatty acid biosynthetic process
A0006637biological_processacyl-CoA metabolic process
A0015645molecular_functionfatty acid ligase activity
A0016405molecular_functionCoA-ligase activity
A0016874molecular_functionligase activity
A0016878molecular_functionacid-thiol ligase activity
A0018858molecular_functionbenzoate-CoA ligase activity
A0031956molecular_functionmedium-chain fatty acid-CoA ligase activity
A0036112biological_processmedium-chain fatty-acyl-CoA metabolic process
A0042593biological_processglucose homeostasis
A0046872molecular_functionmetal ion binding
A0070328biological_processtriglyceride homeostasis
A0102391molecular_functiondecanoate-CoA ligase activity
Functional Information from PDB Data
site_idAC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MG A 601
ChainResidue
AMET483
AHIS485
AVAL488
AHOH1087
AHOH1093
AHOH1094

site_idAC2
Number of Residues1
DetailsBINDING SITE FOR RESIDUE CL A 602
ChainResidue
AARG472

site_idAC3
Number of Residues2
DetailsBINDING SITE FOR RESIDUE CL A 603
ChainResidue
ATHR345
AASN348

site_idAC4
Number of Residues1
DetailsBINDING SITE FOR RESIDUE CL A 604
ChainResidue
AGLN352

site_idAC5
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CL A 605
ChainResidue
ASER301
ASER302
AHOH830

site_idAC6
Number of Residues10
DetailsBINDING SITE FOR RESIDUE GOL A 606
ChainResidue
ASER301
ASER302
ATYR303
APRO304
AGLY399
AASN400
AVAL401
AARG413
AASP440
AHOH989

Functional Information from PROSITE/UniProt
site_idPS00455
Number of Residues12
DetailsAMP_BINDING Putative AMP-binding domain signature. IYFTSGTSGlPK
ChainResidueDetails
AILE218-LYS229

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues9
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"19345228","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues16
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"19345228","evidenceCode":"ECO:0000269"},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"FEB-2008","submissionDatabase":"PDB data bank","title":"Crystal structure of L64P mutant of human acyl-CoA synthetase medium-chain family member 2A.","authoringGroup":["Structural genomics consortium (SGC)"]}}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"Q68CK6","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

246704

PDB entries from 2025-12-24

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