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SummaryStructural detailsExperimental detailsFunctional detailsSequence NeighborHistoryDownloads

5USR

Crystal structure of human NFS1-ISD11 in complex with E. coli acyl-carrier protein at 3.09 angstroms

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
B1990229cellular_componentiron-sulfur cluster assembly complex
C0030170molecular_functionpyridoxal phosphate binding
C0031071molecular_functioncysteine desulfurase activity
C0044571biological_process[2Fe-2S] cluster assembly
D0005198molecular_functionstructural molecule activity
D0005515molecular_functionprotein binding
D0005634cellular_componentnucleus
D0005739cellular_componentmitochondrion
D0005759cellular_componentmitochondrial matrix
D0016226biological_processiron-sulfur cluster assembly
D0016604cellular_componentnuclear body
D0042803molecular_functionprotein homodimerization activity
D0044571biological_process[2Fe-2S] cluster assembly
D0044572biological_process[4Fe-4S] cluster assembly
D0060090molecular_functionmolecular adaptor activity
D0099128cellular_componentmitochondrial [2Fe-2S] assembly complex
D1990221cellular_componentL-cysteine desulfurase complex
D1990229cellular_componentiron-sulfur cluster assembly complex
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
F1990229cellular_componentiron-sulfur cluster assembly complex
G0030170molecular_functionpyridoxal phosphate binding
G0031071molecular_functioncysteine desulfurase activity
G0044571biological_process[2Fe-2S] cluster assembly
H0005198molecular_functionstructural molecule activity
H0005515molecular_functionprotein binding
H0005634cellular_componentnucleus
H0005739cellular_componentmitochondrion
H0005759cellular_componentmitochondrial matrix
H0016226biological_processiron-sulfur cluster assembly
H0016604cellular_componentnuclear body
H0042803molecular_functionprotein homodimerization activity
H0044571biological_process[2Fe-2S] cluster assembly
H0044572biological_process[4Fe-4S] cluster assembly
H0060090molecular_functionmolecular adaptor activity
H0099128cellular_componentmitochondrial [2Fe-2S] assembly complex
H1990221cellular_componentL-cysteine desulfurase complex
H1990229cellular_componentiron-sulfur cluster assembly complex
I0000035molecular_functionacyl binding
I0000036molecular_functionacyl carrier activity
I0005515molecular_functionprotein binding
I0005737cellular_componentcytoplasm
I0005829cellular_componentcytosol
I0006629biological_processlipid metabolic process
I0006631biological_processfatty acid metabolic process
I0006633biological_processfatty acid biosynthetic process
I0008289molecular_functionlipid binding
I0008610biological_processlipid biosynthetic process
I0009245biological_processlipid A biosynthetic process
I0009410biological_processresponse to xenobiotic stimulus
I0016020cellular_componentmembrane
I0031177molecular_functionphosphopantetheine binding
J0000035molecular_functionacyl binding
J0000036molecular_functionacyl carrier activity
J0005515molecular_functionprotein binding
J0005737cellular_componentcytoplasm
J0005829cellular_componentcytosol
J0006629biological_processlipid metabolic process
J0006631biological_processfatty acid metabolic process
J0006633biological_processfatty acid biosynthetic process
J0008289molecular_functionlipid binding
J0008610biological_processlipid biosynthetic process
J0009245biological_processlipid A biosynthetic process
J0009410biological_processresponse to xenobiotic stimulus
J0016020cellular_componentmembrane
J0031177molecular_functionphosphopantetheine binding
K0000035molecular_functionacyl binding
K0000036molecular_functionacyl carrier activity
K0005515molecular_functionprotein binding
K0005737cellular_componentcytoplasm
K0005829cellular_componentcytosol
K0006629biological_processlipid metabolic process
K0006631biological_processfatty acid metabolic process
K0006633biological_processfatty acid biosynthetic process
K0008289molecular_functionlipid binding
K0008610biological_processlipid biosynthetic process
K0009245biological_processlipid A biosynthetic process
K0009410biological_processresponse to xenobiotic stimulus
K0016020cellular_componentmembrane
K0031177molecular_functionphosphopantetheine binding
L0000035molecular_functionacyl binding
L0000036molecular_functionacyl carrier activity
L0005515molecular_functionprotein binding
L0005737cellular_componentcytoplasm
L0005829cellular_componentcytosol
L0006629biological_processlipid metabolic process
L0006631biological_processfatty acid metabolic process
L0006633biological_processfatty acid biosynthetic process
L0008289molecular_functionlipid binding
L0008610biological_processlipid biosynthetic process
L0009245biological_processlipid A biosynthetic process
L0009410biological_processresponse to xenobiotic stimulus
L0016020cellular_componentmembrane
L0031177molecular_functionphosphopantetheine binding
Functional Information from PDB Data
site_idAC1
Number of Residues16
Detailsbinding site for Di-peptide 8Q1 I 101 and SER I 37
ChainResidue
FARG6
FALA59
FASP62
IASP36
ILEU38
IASP39
ITHR40
IVAL41
FLEU10
FMET16
FALA39
FASN43
FLYS44
FVAL46
FILE52
FLEU55
site_idAC2
Number of Residues18
Detailsbinding site for Di-peptide 8Q1 J 101 and SER J 37
ChainResidue
GARG72
HARG6
HVAL9
HLEU10
HALA39
HPHE40
HASN43
HLYS44
HVAL46
HILE52
HLEU55
HLYS58
HASP62
JASP36
JLEU38
JASP39
JTHR40
JVAL41
site_idAC3
Number of Residues15
Detailsbinding site for Di-peptide 8Q1 K 101 and SER K 37
ChainResidue
BARG6
BLEU10
BMET16
BILE36
BALA39
BASN43
BLYS44
BILE52
BLEU55
BALA59
KASP36
KLEU38
KASP39
KTHR40
KVAL41
site_idAC4
Number of Residues14
Detailsbinding site for Di-peptide 8Q1 L 101 and SER L 37
ChainResidue
CARG72
DARG6
DARG35
DILE36
DALA39
DASN43
DLYS44
DVAL46
DLEU55
LASP36
LLEU38
LASP39
LTHR40
LVAL41
Functional Information from PROSITE/UniProt
site_idPS00012
Number of Residues16
DetailsPHOSPHOPANTETHEINE Phosphopantetheine attachment site. DLGADSLDTVELVMAL
ChainResidueDetails
IASP32-LEU47
site_idPS00595
Number of Residues20
DetailsAA_TRANSFER_CLASS_5 Aminotransferases class-V pyridoxal-phosphate attachment site. IDLMsiSGHKiygpk.GvGaI
ChainResidueDetails
AILE249-ILE268
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
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 Residues4
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 Residues16
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 Residues4
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 Residues1
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"29097656","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"5WLW","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI6
Number of Residues4
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 Residues1
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 Residues8
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"31664822","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"6ODD","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI9
Number of Residues4
DetailsModified residue: {"description":"N6-succinyllysine","evidences":[{"source":"UniProtKB","id":"Q8K215","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI10
Number of Residues75
DetailsDomain: {"description":"Carrier","evidences":[{"source":"PROSITE-ProRule","id":"PRU00258","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI11
Number of Residues4
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

243531

PDB entries from 2025-10-22

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