5USR: Human NFS1-ISD11

Crystal structure of human NFS1-ISD11 in complex with E. coli acyl-carrier protein at 3.09 angstroms. Determined by X-ray diffraction at 3.09 Å resolution. Released 21 Jun 2017.

Method: X-ray diffraction
Resolution: 3.09 Å
Organisms: Homo sapiens, Escherichia coli (strain K12)
Chains: 12
Atoms: 15,666
Mol. weight: 270.29 kDa
Ligands: 8Q1
Released: 21 Jun 2017

Explore 5USR in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

5USR contains 91 α-helices and 70 β-strands across 12 chains. Residue ranges use author residue numbering, as in the PDB file, from PDBe. To see them in 3D, choose the Cartoon representation with Secondary structure coloring: helices, sheets and coils get different colors.

Chain A: 19 helices, 18 β-strands

Element	Residues	Length	Sheet
α-helix	64-66	3
α-helix	68-70	3
α-helix	71-84	14
α-helix	95-114	20
α-helix	118-120	3
β-strand	121-124	4	1
α-helix	127-141	15
β-strand	148-152	5	1
α-helix	157-169	13
β-strand	172-176	5	1
β-strand	178	1	2
β-strand	184	1	2
α-helix	186-190	5
β-strand	197-201	5	1
β-strand	205	1	3
β-strand	211	1	4
β-strand	212	1	3
α-helix	215-224	10
β-strand	228-232	5	1
β-strand	251-255	5	1
α-helix	257-259	3
β-strand	266-270	5	1
β-strand	272	1	5
β-strand	275	1	5
α-helix	276	1
α-helix	279-281	3
α-helix	295-297	3
α-helix	298-336	39
β-strand	340-342	3	6
α-helix	346-348	3
β-strand	349	1	4
β-strand	353-358	6	6
α-helix	390-394	5
α-helix	399-403	5
β-strand	405-409	5	6
α-helix	416-434	19
α-helix	439-442	4

Chains B and H: 3 helices, 0 β-strands

Element	Residues	Length
α-helix	6-20	15
α-helix	26-42	17
α-helix	49-76	28

Chain C: 14 helices, 16 β-strands

Element	Residues	Length	Sheet
α-helix	71-82	12
α-helix	98-114	17
α-helix	118-120	3
β-strand	121-124	4	7
α-helix	127-141	15
β-strand	148-152	5	7
α-helix	157-169	13
β-strand	172-176	5	7
β-strand	178	1	8
β-strand	184	1	8
α-helix	186-190	5
β-strand	197-201	5	7
β-strand	205	1	9
β-strand	211	1	10
β-strand	212	1	9
α-helix	215-224	10
β-strand	228-232	5	7
β-strand	251-255	5	7
α-helix	257-259	3
β-strand	266-270	5	7
α-helix	298-336	39
β-strand	340-342	3	11
α-helix	346-348	3
β-strand	349	1	10
β-strand	353-358	6	11
α-helix	364-370	7
α-helix	400-403	4
β-strand	405-409	5	11
α-helix	416-434	19
α-helix	438-441	4

Chain D: 4 helices, 1 β-strand

Element	Residues	Length	Sheet
α-helix	6-20	15
α-helix	26-42	17
α-helix	43-45	3
α-helix	49-76	28
β-strand	82	1	12

Chain E: 13 helices, 16 β-strands

Element	Residues	Length	Sheet
β-strand	54	1	12
α-helix	68-70	3
α-helix	71-83	13
α-helix	97-114	18
α-helix	118-120	3
β-strand	121-124	4	13
α-helix	127-131	5
α-helix	132-136	5
α-helix	137-141	5
β-strand	148-152	5	13
α-helix	157-169	13
β-strand	172-176	5	13
β-strand	178	1	14
β-strand	184	1	14
α-helix	186-190	5
β-strand	197-201	5	13
β-strand	205-206	2	15
β-strand	211-212	2	15
α-helix	215-224	10
β-strand	228-232	5	13
β-strand	251-255	5	13
β-strand	266-270	5	13
α-helix	298-334	37
β-strand	340-342	3	16
α-helix	346-348	3
β-strand	349	1	15
β-strand	353-358	6	16
β-strand	405-409	5	16
α-helix	416-434	19

Chain F: 4 helices, 0 β-strands

Element	Residues	Length
α-helix	6-20	15
α-helix	26-42	17
α-helix	43-45	3
α-helix	49-76	28

Chain G: 13 helices, 15 β-strands

Element	Residues	Length	Sheet
α-helix	68-70	3
α-helix	71-82	12
α-helix	100-114	15
α-helix	118-120	3
β-strand	121-124	4	17
α-helix	127-131	5
α-helix	132-136	5
α-helix	137-141	5
β-strand	148-152	5	17
α-helix	157-169	13
β-strand	172-176	5	17
β-strand	178	1	18
β-strand	184	1	18
α-helix	186-190	5
β-strand	197-201	5	17
β-strand	205-206	2	19
β-strand	211-212	2	19
α-helix	215-224	10
β-strand	228-232	5	17
β-strand	251-255	5	17
α-helix	256-258	3
β-strand	266-270	5	17
α-helix	298-336	39
β-strand	341-342	2	20
β-strand	349	1	19
β-strand	353-357	5	20
β-strand	405-409	5	20
α-helix	416-435	20

Chain I: 5 helices, 2 β-strands

Element	Residues	Length	Sheet
α-helix	6-16	11
β-strand	28	1	21
α-helix	29-32	4
α-helix	37-50	14
α-helix	57-61	5
β-strand	65	1	21
α-helix	66-73	8

3 more chain groups are not listed. Open the entry in the viewer and use the sequence panel to see them.

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Cysteine desulfurase, mitochondrial	A, C, E, G	protein	426	Homo sapiens	Q9Y697 (AlphaFold model)
LYR motif-containing protein 4	B, D, F, H	protein	91	Homo sapiens	Q9HD34 (AlphaFold model)
Acyl carrier protein	I, J, K, L	protein	78	Escherichia coli (strain K12)	P0A6A8 (AlphaFold model)

Sequence of entity 1 (A, C, E, G), FASTA

>5USR_1 Cysteine desulfurase, mitochondrial (chains A, C, E, G)
MGSSHHHHHHSSGLVPRGSHMLEMLRPLYMDVQATTPLDPRVLDAMLPYLINYYGNPHSR
THAYGWESEAAMERARQQVASLIGADPREIIFTSGATESNNIAIKGVARFYRSRKKHLIT
TQTEHKCVLDSCRSLEAEGFQVTYLPVQKSGIIDLKELEAAIQPDTSLVSVMTVNNEIGV
KQPIAEIGRICSSRKVYFHTDAAQAVGKIPLDVNDMKIDLMSISGHKIYGPKGVGAIYIR
RRPRVRVEALQSGGGQERGMRSGTVPTPLVVGLGAACEVAQQEMEYDHKRISKLSERLIQ
NIMKSLPDVVMNGDPKHHYPGCINLSFAYVEGESLLMALKDVALSSGSACTSASLEPSYV
LRAIGTDEDLAHSSIRFGIGRFTTEEEVDYTVEKCIQHVKRLREMSPLWEMVQDGIDLKS
IKWTQH

Sequence of entity 2 (B, D, F, H), FASTA

>5USR_2 LYR motif-containing protein 4 (chains B, D, F, H)
MAASSRAQVLALYRAMLRESKRFSAYNYRTYAVRRIRDAFRENKNVKDPVEIQTLVNKAK
RDLGVIRRQVHIGQLYSTDKLIIENRDMPRT

Sequence of entity 3 (I, J, K, L), FASTA

>5USR_3 Acyl carrier protein (chains I, J, K, L)
MSTIEERVKKIIGEQLGVKQEEVTNNASFVEDLGADSLDTVELVMALEEEFDTEIPDEEA
EKITTVQAAIDYINGHQA

Ligands and cofactors

ID	Name	Formula	Copies
8Q1	S-[2-({N-[(2R)-2-hydroxy-3,3-dimethyl-4-(phosphonooxy)butanoyl]-beta-alanyl}ami…	C23 H45 N2 O8 P S	4

Primary citation

Structure of human Fe-S assembly subcomplex reveals unexpected cysteine desulfurase architecture and acyl-ACP-ISD11 interactions. Cory, S.A., Van Vranken, J.G., Brignole, E.J. et al. Proc Natl Acad Sci U S A (2017) 114:E5325-E5334. DOI 10.1073/pnas.1702849114 · PubMed

Other PDB entries of the same protein (UniProt Q9Y697 (AlphaFold model), which also has an AlphaFold model), best resolution first:

6UXE 1.57 Å, Structure of the human mitochondrial desulfurase complex Nfs1-ISCU2(M140I)-ISD11 with…
6W1D 1.79 Å, Structure of human mitochondrial complex Nfs1-ISCU2 (WT)-ISD11 with E.coli ACP1 at 1.8 A…
6WIH 1.9 Å, N-terminal mutation of ISCU2 (L35H36) traps Nfs1 Cys loop in the active site of ISCU2…
6WI2 1.95 Å, Structure of human mitochondrial complex Nfs1-ISCU2-ISD11 with E.coli ACP1 at 1.95 A…
8TVT 2.0 Å, Structure of human Cysteine desulfurase Nfs1 with L-propargylglycine bound to active…
8RMC 2.26 Å, Structure of the FDX2-bound core ISC complex (proximal conformation)
8RMF 2.33 Å, Structure of the core ISC complex under turnover conditions (FDX2-bound in proximal…
8RMG 2.46 Å, Structure of the core ISC complex under turnover conditions (FDX2-bound in distal…
8PK8 2.49 Å, Structure of the human mitochondrial iron-sulfur cluster biosynthesis complex during…
8RME 2.49 Å, Structure of the core ISC complex under turnover conditions (frataxin-bound)
7RTK 2.5 Å, Structure of the (NIAU)2 complex with N-terminal mutation of ISCU2 Y35D at 2.5 A…
8RMD 2.52 Å, Structure of the FDX2-bound core ISC complex (distal conformation)

Browse structure collections

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