9J7A: Local refinement of FEM1B
local refinement of FEM1B bound with TOM20 (dimer). Determined by electron microscopy at 4.13 Å resolution. Released 9 Apr 2025.
- Method
- Electron microscopy
- Resolution
- 4.13 Å
- Organism
- Homo sapiens
- Chains
- 6
- Atoms
- 11,036
- Mol. weight
- 170.3 kDa
- Released
- 9 Apr 2025
Explore 9J7A in 3D
Show helices and sheets
RCSB PDB
PDBe
Secondary structure: helices and β-sheets
9J7A contains 85 α-helices and 6 β-strands across 6 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: 40 helices, 2 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 2-13 | 12 | |
| α-helix | 17-22 | 6 | |
| α-helix | 29-36 | 8 | |
| α-helix | 42-44 | 3 | |
| α-helix | 49-56 | 8 | |
| α-helix | 59-62 | 4 | |
| α-helix | 63-67 | 5 | |
| α-helix | 91-98 | 8 | |
| α-helix | 101-110 | 10 | |
| α-helix | 124-131 | 8 | |
| α-helix | 134-142 | 9 | |
| α-helix | 157-163 | 7 | |
| α-helix | 167-175 | 9 | |
| α-helix | 200-208 | 9 | |
| α-helix | 222-228 | 7 | |
| α-helix | 232-239 | 8 | |
| α-helix | 246-261 | 16 | |
| α-helix | 269-283 | 15 | |
| α-helix | 293-295 | 3 | |
| α-helix | 300-302 | 3 | |
| α-helix | 311-316 | 6 | |
| α-helix | 321-331 | 11 | |
| α-helix | 332-336 | 5 | |
| α-helix | 341-343 | 3 | |
| α-helix | 344-356 | 13 | |
| α-helix | 360-376 | 17 | |
| α-helix | 382-397 | 16 | |
| α-helix | 404-427 | 24 | |
| α-helix | 433-455 | 23 | |
| α-helix | 462-477 | 16 | |
| α-helix | 487-492 | 6 | |
| α-helix | 502-505 | 4 | |
| α-helix | 511 | 1 | |
| α-helix | 512-520 | 9 | |
| α-helix | 535-539 | 5 | |
| α-helix | 546-548 | 3 | |
| α-helix | 549-561 | 13 | |
| β-strand | 570 | 1 | 1 |
| β-strand | 574 | 1 | 1 |
| α-helix | 583-592 | 10 | |
| α-helix | 597-607 | 11 | |
| α-helix | 618-626 | 9 | |
Chain B: 5 helices, 0 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 64-83 | 20 | |
| α-helix | 86-100 | 15 | |
| α-helix | 104-109 | 6 | |
| α-helix | 110-112 | 3 | |
| α-helix | 116-124 | 9 | |
Chain C: 4 helices, 0 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 68-82 | 15 | |
| α-helix | 86-99 | 14 | |
| α-helix | 103-113 | 11 | |
| α-helix | 116-125 | 10 | |
Chain D: 34 helices, 4 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 2-13 | 12 | |
| α-helix | 17-25 | 9 | |
| α-helix | 29-35 | 7 | |
| α-helix | 49-56 | 8 | |
| α-helix | 59-68 | 10 | |
| β-strand | 77-81 | 5 | 2 |
| β-strand | 84-89 | 6 | 2 |
| α-helix | 91-98 | 8 | |
| α-helix | 101-110 | 10 | |
| α-helix | 124-131 | 8 | |
| α-helix | 134-142 | 9 | |
| α-helix | 157-163 | 7 | |
| α-helix | 167-175 | 9 | |
| α-helix | 190-197 | 8 | |
| α-helix | 200-208 | 9 | |
| α-helix | 222-228 | 7 | |
| α-helix | 232-239 | 8 | |
| α-helix | 246-261 | 16 | |
| α-helix | 269-284 | 16 | |
| α-helix | 300-302 | 3 | |
| α-helix | 311-316 | 6 | |
| α-helix | 321-336 | 16 | |
| α-helix | 345-356 | 12 | |
| α-helix | 360-376 | 17 | |
| α-helix | 382-397 | 16 | |
| α-helix | 404-427 | 24 | |
| α-helix | 433-456 | 24 | |
| α-helix | 461-477 | 17 | |
| α-helix | 487-492 | 6 | |
| α-helix | 503-506 | 4 | |
| α-helix | 512-521 | 10 | |
| β-strand | 528 | 1 | 3 |
| β-strand | 534 | 1 | 3 |
| α-helix | 535-540 | 6 | |
| α-helix | 549-562 | 14 | |
| α-helix | 583-592 | 10 | |
| α-helix | 597-607 | 11 | |
| α-helix | 618-626 | 9 | |
Chain E: 1 helix, 0 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 3-9 | 7 | |
Chain F: 1 helix, 0 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 4-10 | 7 | |
Molecules and chains
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|
| Protein fem-1 homolog B | A, D | protein | 627 | Homo sapiens | Q9UK73 (AlphaFold model) |
| Mitochondrial import receptor subunit TOM20 homolog | B, C | protein | 121 | Homo sapiens | Q15388 (AlphaFold model) |
| Poly-UNK | E, F | protein | 11 | Homo sapiens | |
Sequence of entity 1 (A, D), FASTA
>9J7A_1 Protein fem-1 homolog B (chains A, D)
MEGLAGYVYKAASEGKVLTLAALLLNRSESDIRYLLGYVSQQGGQRSTPLIIAARNGHAK
VVRLLLEHYRVQTQQTGTVRFDGYVIDGATALWCAAGAGHFEVVKLLVSHGANVNHTTVT
NSTPLRAACFDGRLDIVKYLVENNANISIANKYDNTCLMIAAYKGHTDVVRYLLEQRADP
NAKAHCGATALHFAAEAGHIDIVKELIKWRAAIVVNGHGMTPLKVAAESCKADVVELLLS
HADCDRRSRIEALELLGASFANDRENYDIIKTYHYLYLAMLERFQDGDNILEKEVLPPIH
AYGNRTECRNPQELESIRQDRDALHMEGLIVRERILGADNIDVSHPIIYRGAVYADNMEF
EQCIKLWLHALHLRQKGNRNTHKDLLRFAQVFSQMIHLNETVKAPDIECVLRCSVLEIEQ
SMNRVKNISDADVHNAMDNYECNLYTFLYLVCISTKTQCSEEDQCKINKQIYNLIHLDPR
TREGFTLLHLAVNSNTPVDDFHTNDVCSFPNALVTKLLLDCGAEVNAVDNEGNSALHIIV
QYNRPISDFLTLHSIIISLVEAGAHTDMTNKQNKTPLDKSTTGVSEILLKTQMKMSLKCL
AARAVRANDINYQDQIPRTLEEFVGFH
Sequence of entity 2 (B, C), FASTA
>9J7A_2 Mitochondrial import receptor subunit TOM20 homolog (chains B, C)
DRKRRSDPNFKNRLRERRKKQKLAKERAGLSKLPDLKDAEAVQKFFLEEIQLGEELLAQG
EYEKGVDHLTNAIAVCGQPQQLLQVLQQTLPPPVFQMLLTKLPTISQRIVSAQSLAEDDV
E
Sequence of entity 3 (E, F), FASTA
>9J7A_3 Poly-UNK (chains E, F)
XXXXXXXXXXX
Primary citation
TOM20-driven E3 ligase recruitment regulates mitochondrial dynamics through PLD6. Raiff, A., Zhao, S., Bekturova, A. et al. Nat Chem Biol (2026) 22:37-47. DOI 10.1038/s41589-025-01894-4 · PubMed
Other PDB entries of the same protein (UniProt Q9UK73 (AlphaFold model), which also has an AlphaFold model), best resolution first:
- 9PW8 2.8 Å, Fem-1 homolog B (FEM1B) in complex with VU0417412
- 7EL6 2.8 Å, Structure of SMCR8 bound FEM1B
- 9PQA 2.9 Å, Fem-1 homolog B (FEM1B) in complex with VU0432623
- 9PQ9 2.93 Å, Fem-1 homolog B (FEM1B) in complex with VU0421763
- 9PWJ 3.0 Å, Fem-1 homolog B (FEM1B) in complex with VU0081201
- 9PXP 3.0 Å, Fem-1 homolog B (FEM1B) in complex with VU0416476
- 9PXO 3.05 Å, Fem-1 homolog B (FEM1B) in complex with VU0023775
- 9PQE 3.1 Å, Fem-1 homolog B (FEM1B) in complex with VU0412674
- 6LBF 3.25 Å, Crystal structure of FEM1B
- 8WQF 3.27 Å, cryo-EM structure of CUL2-RBX1-ELOB-ELOC-FEM1B bound with the C-degron of CUX1…
- 8WQB 3.37 Å, Cryo-EM structure of CUL2-RBX1-ELOB-ELOC-FEM1B bound with the C-degron of CCDC89…
- 8WQE 3.38 Å, Cryo-EM structure of CUL2-RBX1-ELOB-ELOC-FEM1B bound with the C-degron of CUX1…
Browse structure collections
About this viewer
MolViewer shows 9J7A 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.