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 | Sheet |
|---|
| 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 | Sheet |
|---|
| 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
About this viewer
MolViewer shows 5USR directly in your browser with nothing to install. Switch between cartoon, ball-and-stick, spacefill and surface views, color by chain, secondary structure or B-factor, measure distances, angles and dihedrals, and share or embed the view.