9J7B: Local refinement of FEM1B
local refinement of FEM1B bound with TOM20(tetramer). Determined by electron microscopy at 4.12 Å resolution. Released 9 Apr 2025.
- Method
- Electron microscopy
- Resolution
- 4.12 Å
- Organism
- Homo sapiens
- Chains
- 11
- Atoms
- 20,578
- Mol. weight
- 352.44 kDa
- Released
- 9 Apr 2025
Explore 9J7B in 3D
Show helices and sheets
RCSB PDB
PDBe
Secondary structure: helices and β-sheets
9J7B contains 158 α-helices and 16 β-strands across 10 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: 34 helices, 4 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 2-14 | 13 | |
| α-helix | 18-23 | 6 | |
| α-helix | 29-36 | 8 | |
| β-strand | 41-42 | 2 | 3 |
| β-strand | 45-46 | 2 | 3 |
| α-helix | 49-56 | 8 | |
| α-helix | 59-67 | 9 | |
| 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 | 311-316 | 6 | |
| α-helix | 321-336 | 16 | |
| α-helix | 341-343 | 3 | |
| α-helix | 344-356 | 13 | |
| α-helix | 360-377 | 18 | |
| 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 | 512-520 | 9 | |
| α-helix | 535-540 | 6 | |
| α-helix | 549-560 | 12 | |
| β-strand | 570 | 1 | 4 |
| β-strand | 574 | 1 | 4 |
| α-helix | 578-580 | 3 | |
| α-helix | 583-592 | 10 | |
| α-helix | 603-607 | 5 | |
| α-helix | 618-626 | 9 | |
Chain B: 5 helices, 0 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 68-83 | 16 | |
| α-helix | 86-99 | 14 | |
| α-helix | 104-106 | 3 | |
| α-helix | 107-110 | 4 | |
| α-helix | 116-124 | 9 | |
Chain C: 4 helices, 0 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 67-82 | 16 | |
| α-helix | 86-99 | 14 | |
| α-helix | 105-112 | 8 | |
| α-helix | 116-125 | 10 | |
Chain D: 1 helix, 0 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 3-8 | 6 | |
Chain G: 1 helix, 0 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 5-7 | 3 | |
Chain J: 36 helices, 4 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 2-14 | 13 | |
| α-helix | 17-22 | 6 | |
| α-helix | 29-36 | 8 | |
| α-helix | 49-55 | 7 | |
| α-helix | 59-68 | 10 | |
| β-strand | 77-80 | 4 | 1 |
| β-strand | 85-88 | 4 | 1 |
| α-helix | 91-98 | 8 | |
| α-helix | 102-109 | 8 | |
| α-helix | 124-131 | 8 | |
| α-helix | 134-142 | 9 | |
| β-strand | 150 | 1 | 2 |
| β-strand | 156 | 1 | 2 |
| α-helix | 157-163 | 7 | |
| α-helix | 167-175 | 9 | |
| α-helix | 190-197 | 8 | |
| α-helix | 200-209 | 10 | |
| α-helix | 222-226 | 5 | |
| α-helix | 232-241 | 10 | |
| α-helix | 246-261 | 16 | |
| α-helix | 269-284 | 16 | |
| α-helix | 293-295 | 3 | |
| α-helix | 297-299 | 3 | |
| α-helix | 311-317 | 7 | |
| α-helix | 321-336 | 16 | |
| α-helix | 345-356 | 12 | |
| α-helix | 360-376 | 17 | |
| α-helix | 383-397 | 15 | |
| α-helix | 401-403 | 3 | |
| 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 | |
| α-helix | 535-540 | 6 | |
| α-helix | 549-562 | 14 | |
| α-helix | 583-591 | 9 | |
| α-helix | 597-608 | 12 | |
| α-helix | 618-626 | 9 | |
Chain O: 34 helices, 6 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 3-13 | 11 | |
| α-helix | 17-24 | 8 | |
| α-helix | 30-37 | 8 | |
| α-helix | 42-44 | 3 | |
| α-helix | 49-55 | 7 | |
| α-helix | 59-68 | 10 | |
| β-strand | 76 | 1 | 5 |
| β-strand | 79-80 | 2 | 6 |
| β-strand | 85-86 | 2 | 6 |
| β-strand | 90 | 1 | 5 |
| α-helix | 91-97 | 7 | |
| α-helix | 101-110 | 10 | |
| α-helix | 124-131 | 8 | |
| α-helix | 134-142 | 9 | |
| β-strand | 150 | 1 | 7 |
| β-strand | 156 | 1 | 7 |
| α-helix | 157-161 | 5 | |
| α-helix | 167-175 | 9 | |
| α-helix | 190-196 | 7 | |
| α-helix | 200-209 | 10 | |
| α-helix | 222-227 | 6 | |
| α-helix | 233-240 | 8 | |
| α-helix | 246-259 | 14 | |
| α-helix | 269-283 | 15 | |
| α-helix | 297-299 | 3 | |
| α-helix | 313-316 | 4 | |
| α-helix | 321-336 | 16 | |
| α-helix | 341-356 | 16 | |
| α-helix | 360-377 | 18 | |
| α-helix | 382-397 | 16 | |
| α-helix | 401-403 | 3 | |
| 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 | 512-520 | 9 | |
| α-helix | 535-540 | 6 | |
| α-helix | 549-562 | 14 | |
| α-helix | 583-591 | 9 | |
Chain P: 34 helices, 2 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 2-13 | 12 | |
| α-helix | 17-24 | 8 | |
| α-helix | 29-37 | 9 | |
| α-helix | 49-56 | 8 | |
| α-helix | 59-64 | 6 | |
| α-helix | 81-83 | 3 | |
| α-helix | 91-97 | 7 | |
| α-helix | 101-110 | 10 | |
| α-helix | 124-131 | 8 | |
| α-helix | 134-143 | 10 | |
| β-strand | 150 | 1 | 8 |
| β-strand | 156 | 1 | 8 |
| α-helix | 157-163 | 7 | |
| α-helix | 167-173 | 7 | |
| α-helix | 200-208 | 9 | |
| α-helix | 222-228 | 7 | |
| α-helix | 232-239 | 8 | |
| α-helix | 246-260 | 15 | |
| α-helix | 269-283 | 15 | |
| α-helix | 296-298 | 3 | |
| α-helix | 311-316 | 6 | |
| α-helix | 321-336 | 16 | |
| α-helix | 341-356 | 16 | |
| α-helix | 360-376 | 17 | |
| α-helix | 382-397 | 16 | |
| α-helix | 401-403 | 3 | |
| α-helix | 404-427 | 24 | |
| α-helix | 434-456 | 23 | |
| α-helix | 461-477 | 17 | |
| α-helix | 487-490 | 4 | |
| α-helix | 502-504 | 3 | |
| α-helix | 512-521 | 10 | |
| α-helix | 535-541 | 7 | |
| α-helix | 544-547 | 4 | |
| α-helix | 549-554 | 6 | |
| α-helix | 556-559 | 4 | |
2 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 |
|---|
| Protein fem-1 homolog B | A, J, O, P | protein | 627 | Homo sapiens | Q9UK73 (AlphaFold model) |
| Mitochondrial import receptor subunit TOM20 homolog | B, C, G, Q, S | protein | 121 | Homo sapiens | Q15388 (AlphaFold model) |
| Poly-UNK | D | protein | 12 | Homo sapiens | |
| Poly-UNK | R | protein | 9 | Homo sapiens | |
Sequence of entity 1 (A, J, O, P), FASTA
>9J7B_1 Protein fem-1 homolog B (chains A, J, O, P)
MEGLAGYVYKAASEGKVLTLAALLLNRSESDIRYLLGYVSQQGGQRSTPLIIAARNGHAK
VVRLLLEHYRVQTQQTGTVRFDGYVIDGATALWCAAGAGHFEVVKLLVSHGANVNHTTVT
NSTPLRAACFDGRLDIVKYLVENNANISIANKYDNTCLMIAAYKGHTDVVRYLLEQRADP
NAKAHCGATALHFAAEAGHIDIVKELIKWRAAIVVNGHGMTPLKVAAESCKADVVELLLS
HADCDRRSRIEALELLGASFANDRENYDIIKTYHYLYLAMLERFQDGDNILEKEVLPPIH
AYGNRTECRNPQELESIRQDRDALHMEGLIVRERILGADNIDVSHPIIYRGAVYADNMEF
EQCIKLWLHALHLRQKGNRNTHKDLLRFAQVFSQMIHLNETVKAPDIECVLRCSVLEIEQ
SMNRVKNISDADVHNAMDNYECNLYTFLYLVCISTKTQCSEEDQCKINKQIYNLIHLDPR
TREGFTLLHLAVNSNTPVDDFHTNDVCSFPNALVTKLLLDCGAEVNAVDNEGNSALHIIV
QYNRPISDFLTLHSIIISLVEAGAHTDMTNKQNKTPLDKSTTGVSEILLKTQMKMSLKCL
AARAVRANDINYQDQIPRTLEEFVGFH
Sequence of entity 2 (B, C, G, Q, S), FASTA
>9J7B_2 Mitochondrial import receptor subunit TOM20 homolog (chains B, C, G, Q, S)
DRKRRSDPNFKNRLRERRKKQKLAKERAGLSKLPDLKDAEAVQKFFLEEIQLGEELLAQG
EYEKGVDHLTNAIAVCGQPQQLLQVLQQTLPPPVFQMLLTKLPTISQRIVSAQSLAEDDV
E
Sequence of entity 3 (D), FASTA
>9J7B_3 Poly-UNK (chains D)
XXXXXXXXXXXX
Sequence of entity 4 (R), FASTA
>9J7B_4 Poly-UNK (chains R)
XXXXXXXXX
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 9J7B 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.