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SummaryStructural detailsExperimental detailsFunctional detailsSequence NeighborHistoryDownloads

8RMF

Structure of the core ISC complex under turnover conditions (FDX2-bound in proximal conformation)

Functional Information from GO Data
ChainGOidnamespacecontents
A0030170molecular_functionpyridoxal phosphate binding
A0031071molecular_functioncysteine desulfurase activity
A0044571biological_process[2Fe-2S] cluster assembly
B0005198molecular_functionstructural molecule activity
B0005515molecular_functionprotein binding
B0005634cellular_componentnucleus
B0005739cellular_componentmitochondrion
B0005759cellular_componentmitochondrial matrix
B0016226biological_processiron-sulfur cluster assembly
B0016604cellular_componentnuclear body
B0042803molecular_functionprotein homodimerization activity
B0044571biological_process[2Fe-2S] cluster assembly
B0044572biological_process[4Fe-4S] cluster assembly
B0060090molecular_functionmolecular adaptor activity
B0099128cellular_componentmitochondrial [2Fe-2S] assembly complex
B1990221cellular_componentL-cysteine desulfurase complex
C0000035molecular_functionacyl binding
C0000036molecular_functionacyl carrier activity
C0005515molecular_functionprotein binding
C0005737cellular_componentcytoplasm
C0005829cellular_componentcytosol
C0006629biological_processlipid metabolic process
C0006631biological_processfatty acid metabolic process
C0006633biological_processfatty acid biosynthetic process
C0008289molecular_functionlipid binding
C0008610biological_processlipid biosynthetic process
C0009245biological_processlipid A biosynthetic process
C0009410biological_processresponse to xenobiotic stimulus
C0016020cellular_componentmembrane
C0031177molecular_functionphosphopantetheine binding
D0005506molecular_functioniron ion binding
D0016226biological_processiron-sulfur cluster assembly
D0051536molecular_functioniron-sulfur cluster binding
E0030170molecular_functionpyridoxal phosphate binding
E0031071molecular_functioncysteine desulfurase activity
E0044571biological_process[2Fe-2S] cluster assembly
F0005198molecular_functionstructural molecule activity
F0005515molecular_functionprotein binding
F0005634cellular_componentnucleus
F0005739cellular_componentmitochondrion
F0005759cellular_componentmitochondrial matrix
F0016226biological_processiron-sulfur cluster assembly
F0016604cellular_componentnuclear body
F0042803molecular_functionprotein homodimerization activity
F0044571biological_process[2Fe-2S] cluster assembly
F0044572biological_process[4Fe-4S] cluster assembly
F0060090molecular_functionmolecular adaptor activity
F0099128cellular_componentmitochondrial [2Fe-2S] assembly complex
F1990221cellular_componentL-cysteine desulfurase complex
G0000035molecular_functionacyl binding
G0000036molecular_functionacyl carrier activity
G0005515molecular_functionprotein binding
G0005737cellular_componentcytoplasm
G0005829cellular_componentcytosol
G0006629biological_processlipid metabolic process
G0006631biological_processfatty acid metabolic process
G0006633biological_processfatty acid biosynthetic process
G0008289molecular_functionlipid binding
G0008610biological_processlipid biosynthetic process
G0009245biological_processlipid A biosynthetic process
G0009410biological_processresponse to xenobiotic stimulus
G0016020cellular_componentmembrane
G0031177molecular_functionphosphopantetheine binding
H0005506molecular_functioniron ion binding
H0016226biological_processiron-sulfur cluster assembly
H0051536molecular_functioniron-sulfur cluster binding
I0051536molecular_functioniron-sulfur cluster binding
I0051537molecular_function2 iron, 2 sulfur cluster binding
I0140647biological_processP450-containing electron transport chain
Functional Information from PROSITE/UniProt
site_idPS00012
Number of Residues16
DetailsPHOSPHOPANTETHEINE Phosphopantetheine attachment site. DLGADSLDTVELVMAL
ChainResidueDetails
CASP32-LEU47
site_idPS00595
Number of Residues20
DetailsAA_TRANSFER_CLASS_5 Aminotransferases class-V pyridoxal-phosphate attachment site. IDLMsiSGHKiygpk.GvGaI
ChainResidueDetails
AILE249-ILE268
site_idPS00814
Number of Residues11
DetailsADX Adrenodoxin family, iron-sulfur binding region signature. CeaSlACSTCH
ChainResidueDetails
ICYS108-HIS118
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsActive site: {"description":"Cysteine persulfide intermediate","evidences":[{"source":"PubMed","id":"18650437","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"23593335","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails
site_idSWS_FT_FI2
Number of Residues2
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"29097656","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"34824239","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"5WKP","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5WLW","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6UXE","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6W1D","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6WI2","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6WIH","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"7RTK","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI3
Number of Residues8
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"29097656","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"31101807","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"34824239","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"5WKP","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5WLW","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6NZU","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6UXE","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6W1D","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6WI2","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6WIH","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"7RTK","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI4
Number of Residues2
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"29097656","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"31101807","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"5WKP","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5WLW","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6NZU","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI5
Number of Residues8
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"29097656","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"5WLW","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI6
Number of Residues2
DetailsModified residue: {"description":"N6-(pyridoxal phosphate)lysine","evidences":[{"source":"PubMed","id":"29097656","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"31101807","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"34824239","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"5WKP","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5WLW","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6NZU","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6UXE","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6W1D","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6WI2","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6WIH","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"7RTK","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI7
Number of Residues2
DetailsModified residue: {"description":"Cysteine persulfide","evidences":[{"source":"PubMed","id":"18650437","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"23593335","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails
site_idSWS_FT_FI8
Number of Residues4
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"31664822","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"6ODD","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI9
Number of Residues2
DetailsModified residue: {"description":"N6-succinyllysine","evidences":[{"source":"UniProtKB","id":"Q8K215","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI10
Number of Residues2
DetailsModified residue: {"description":"O-(pantetheine 4'-phosphoryl)serine","evidences":[{"source":"PROSITE-ProRule","id":"PRU00258","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"4882207","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI11
Number of Residues2
DetailsActive site: {"description":"Cysteine persulfide intermediate","evidences":[{"source":"UniProtKB","id":"Q9D7P6","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI12
Number of Residues2
DetailsActive site: {"description":"Cysteine persulfide intermediate","evidences":[{"source":"UniProtKB","id":"O29689","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI13
Number of Residues6
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"31101807","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"6NZU","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI14
Number of Residues2
DetailsSite: {"description":"Mediates ISCU dimerization and de novo [2Fe-2S] cluster assembly","evidences":[{"source":"PubMed","id":"34824239","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI15
Number of Residues2
DetailsModified residue: {"description":"Cysteine persulfide","evidences":[{"source":"UniProtKB","id":"Q9D7P6","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI16
Number of Residues2
DetailsModified residue: {"description":"Cysteine persulfide","evidences":[{"source":"PubMed","id":"24971490","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails
site_idSWS_FT_FI17
Number of Residues102
DetailsDomain: {"description":"2Fe-2S ferredoxin-type","evidences":[{"source":"PROSITE-ProRule","id":"PRU00465","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI18
Number of Residues4
DetailsBinding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00465","evidenceCode":"ECO:0000255"},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"JAN-2011","submissionDatabase":"PDB data bank","title":"Structure and functional studies on human mitochondrial ferredoxins.","authors":["Webert H.","Hobler A.","Sheftel A.D.","Molik S.","Maestre-Reyna M.","Essen L.-O.","Vorniscescu D.","Keusgen M.","Hannemann F.","Bernhardt R.","Lill R."]}},{"source":"PDB","id":"2Y5C","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

247536

PDB entries from 2026-01-14

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