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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
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
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
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
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
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
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
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
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
I0006633biological_processfatty acid biosynthetic process
I0008289molecular_functionlipid binding
I0008610biological_processlipid biosynthetic process
I0009245biological_processlipid A biosynthetic process
I0009410biological_processresponse to xenobiotic stimulus
I0031177molecular_functionphosphopantetheine binding
J0000035molecular_functionacyl binding
J0000036molecular_functionacyl carrier activity
J0005515molecular_functionprotein binding
J0005737cellular_componentcytoplasm
J0005829cellular_componentcytosol
J0006633biological_processfatty acid biosynthetic process
J0008289molecular_functionlipid binding
J0008610biological_processlipid biosynthetic process
J0009245biological_processlipid A biosynthetic process
J0009410biological_processresponse to xenobiotic stimulus
J0031177molecular_functionphosphopantetheine binding
K0000035molecular_functionacyl binding
K0000036molecular_functionacyl carrier activity
K0005515molecular_functionprotein binding
K0005737cellular_componentcytoplasm
K0005829cellular_componentcytosol
K0006633biological_processfatty acid biosynthetic process
K0008289molecular_functionlipid binding
K0008610biological_processlipid biosynthetic process
K0009245biological_processlipid A biosynthetic process
K0009410biological_processresponse to xenobiotic stimulus
K0031177molecular_functionphosphopantetheine binding
L0000035molecular_functionacyl binding
L0000036molecular_functionacyl carrier activity
L0005515molecular_functionprotein binding
L0005737cellular_componentcytoplasm
L0005829cellular_componentcytosol
L0006633biological_processfatty acid biosynthetic process
L0008289molecular_functionlipid binding
L0008610biological_processlipid biosynthetic process
L0009245biological_processlipid A biosynthetic process
L0009410biological_processresponse to xenobiotic stimulus
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 Residues4
DetailsMOD_RES: O-(pantetheine 4'-phosphoryl)serine => ECO:0000255|PROSITE-ProRule:PRU00258, ECO:0000269|PubMed:4882207
ChainResidueDetails
ISER37
JSER37
KSER37
LSER37
FARG6
FLYS44
HARG6
HLYS44

site_idSWS_FT_FI2
Number of Residues4
DetailsMOD_RES: N6-succinyllysine => ECO:0000250|UniProtKB:Q8K215
ChainResidueDetails
BLYS47
DLYS47
FLYS47
HLYS47

site_idSWS_FT_FI3
Number of Residues16
DetailsBINDING: BINDING => ECO:0000269|PubMed:29097656, ECO:0000269|PubMed:31101807, ECO:0000269|PubMed:34824239, ECO:0007744|PDB:5WKP, ECO:0007744|PDB:5WLW, ECO:0007744|PDB:6NZU, ECO:0007744|PDB:6UXE, ECO:0007744|PDB:6W1D, ECO:0007744|PDB:6WI2, ECO:0007744|PDB:6WIH, ECO:0007744|PDB:7RTK
ChainResidueDetails
ATHR128
EGLN235
ESER255
EHIS257
GTHR128
GGLN235
GSER255
GHIS257
AGLN235
ASER255
AHIS257
CTHR128
CGLN235
CSER255
CHIS257
ETHR128

site_idSWS_FT_FI4
Number of Residues4
DetailsBINDING: BINDING => ECO:0000269|PubMed:29097656, ECO:0000269|PubMed:31101807, ECO:0007744|PDB:5WKP, ECO:0007744|PDB:5WLW, ECO:0007744|PDB:6NZU
ChainResidueDetails
ATHR295
CTHR295
ETHR295
GTHR295

site_idSWS_FT_FI5
Number of Residues4
DetailsBINDING: BINDING => ECO:0000269|PubMed:29097656, ECO:0007744|PDB:5WLW
ChainResidueDetails
ACYS381
CCYS381
ECYS381
GCYS381

site_idSWS_FT_FI6
Number of Residues4
DetailsMOD_RES: N6-(pyridoxal phosphate)lysine => ECO:0000269|PubMed:29097656, ECO:0000269|PubMed:31101807, ECO:0000269|PubMed:34824239, ECO:0007744|PDB:5WKP, ECO:0007744|PDB:5WLW, ECO:0007744|PDB:6NZU, ECO:0007744|PDB:6UXE, ECO:0007744|PDB:6W1D, ECO:0007744|PDB:6WI2, ECO:0007744|PDB:6WIH, ECO:0007744|PDB:7RTK
ChainResidueDetails
ALLP258
CLLP258
ELLP258
GLLP258

site_idSWS_FT_FI7
Number of Residues4
DetailsMOD_RES: Cysteine persulfide => ECO:0000305|PubMed:18650437, ECO:0000305|PubMed:23593335
ChainResidueDetails
ACYS381
CCYS381
ECYS381
GCYS381

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PDB entries from 2024-08-28

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