8UY3: Fem1B with FNIP1 and Tom20 fragment

Fem1B with FNIP1 and Tom20 fragment. Determined by X-ray diffraction at 3.2 Å resolution. Released 19 Mar 2025.

Method: X-ray diffraction
Resolution: 3.2 Å
Organisms: Mus musculus, Homo sapiens
Chains: 11
Atoms: 13,741
Mol. weight: 206.61 kDa
Ligands: ZN, PO4
Released: 19 Mar 2025

Explore 8UY3 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

8UY3 contains 108 α-helices and 23 β-strands across 7 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: 24 helices, 4 β-strands

Element	Residues	Length	Sheet
α-helix	0-14	15
α-helix	17-23	7
α-helix	29-37	9
α-helix	49-56	8
α-helix	59-67	9
β-strand	77-81	5	1
β-strand	84-89	6	1
α-helix	91-98	8
α-helix	101-109	9
α-helix	124-131	8
α-helix	134-142	9
α-helix	157-164	8
α-helix	167-175	9
α-helix	190-197	8
α-helix	200-208	9
α-helix	222-228	7
α-helix	232-241	10
α-helix	246-259	14
α-helix	269-283	15
α-helix	295-298	4
β-strand	299	1	2
α-helix	300-302	3
β-strand	305	1	2
α-helix	306-308	3
α-helix	311-316	6
α-helix	321-336	16
α-helix	344-356	13
α-helix	360-374	15

Chain B: 24 helices, 7 β-strands

Element	Residues	Length	Sheet
α-helix	1-13	13
α-helix	17-23	7
α-helix	29-36	8
β-strand	42	1	5
β-strand	45	1	5
β-strand	46	1	6
α-helix	49-56	8
α-helix	59-68	10
β-strand	76-81	6	6
β-strand	84-90	7	6
α-helix	91-98	8
α-helix	101-109	9
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	232-241	10
α-helix	246-259	14
α-helix	269-283	15
α-helix	295-298	4
β-strand	299	1	7
α-helix	300-302	3
β-strand	305	1	7
α-helix	306-308	3
α-helix	311-316	6
α-helix	321-336	16
α-helix	345-356	12
α-helix	360-374	15

Chain C: 24 helices, 6 β-strands

Element	Residues	Length	Sheet
α-helix	2-14	13
α-helix	17-23	7
α-helix	29-35	7
β-strand	40-42	3	3
β-strand	45-47	3	3
α-helix	49-55	7
α-helix	59-68	10
β-strand	77-81	5	3
β-strand	84-89	6	3
α-helix	91-98	8
α-helix	101-109	9
α-helix	124-131	8
α-helix	134-142	9
α-helix	157-164	8
α-helix	167-175	9
α-helix	190-196	7
α-helix	200-208	9
α-helix	222-228	7
α-helix	232-240	9
α-helix	246-260	15
α-helix	269-283	15
α-helix	295-298	4
β-strand	299	1	4
α-helix	300-302	3
β-strand	305	1	4
α-helix	306-308	3
α-helix	311-316	6
α-helix	321-336	16
α-helix	345-356	12
α-helix	360-374	15

Chain D: 24 helices, 6 β-strands

Element	Residues	Length	Sheet
α-helix	5-12	8
α-helix	17-23	7
α-helix	29-37	9
β-strand	40-42	3	8
β-strand	45-47	3	8
α-helix	49-56	8
α-helix	59-68	10
β-strand	76-81	6	9
β-strand	84-90	7	9
α-helix	91-98	8
α-helix	101-109	9
α-helix	124-131	8
α-helix	134-142	9
α-helix	157-163	7
α-helix	167-176	10
α-helix	190-196	7
α-helix	200-208	9
α-helix	222-228	7
α-helix	232-238	7
α-helix	246-259	14
α-helix	269-283	15
α-helix	296-298	3
β-strand	299	1	10
α-helix	300-302	3
β-strand	305	1	10
α-helix	306-308	3
α-helix	311-316	6
α-helix	321-336	16
α-helix	345-356	12
α-helix	360-375	16

Chain J: 4 helices, 0 β-strands

Element	Residues	Length
α-helix	63-83	21
α-helix	86-98	13
α-helix	104-113	10
α-helix	116-124	9

Chain K: 4 helices, 0 β-strands

Element	Residues	Length
α-helix	67-83	17
α-helix	86-98	13
α-helix	104-112	9
α-helix	116-125	10

Chain M: 4 helices, 0 β-strands

Element	Residues	Length
α-helix	67-83	17
α-helix	86-100	15
α-helix	107-113	7
α-helix	116-125	10

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Protein fem-1 homolog B	A, B, C, D	protein	381	Mus musculus	Q9Z2G0 (AlphaFold model)
Folliculin-interacting protein 1	E, F, H, I	protein	31	Mus musculus	Q68FD7 (AlphaFold model)
Mitochondrial import receptor subunit TOM20 homolog	J, K, M	protein	66	Homo sapiens	Q15388 (AlphaFold model)

Sequence of entity 1 (A, B, C, D), FASTA

>8UY3_1 Protein fem-1 homolog B (chains A, B, C, D)
SGSSMEGLAGYVYKAASEGKVLTLAALLLNRSESDIRYLLGYVSQQGGQRSTPLIIAARN
GHAKVVRLLLEHYRVQTQQTGTVRFDGYVIDGATALWCAAGAGHFEVVKLLVSHGANVNH
TTVTNSTPLRAACFDGRLDIVKYLVENNANISIANKYDNTCLMIAAYKGHTDVVRYLLEQ
RADPNAKAHCGATALHFAAEAGHIDIVKELIKWRAAIVVNGHGMTPLKVAAESCKADVVE
LLLSHADCDRRSRIEALELLGASFANDRENYDIMKTYHYLYLAMLERFQDGDNILEKEVL
PPIHAYGNRTECRNPQELEAIRQDRDALHMEGLIVRERILGADNIDVSHPIIYRGAVYAD
NMEFEQCIKLWLHALHLRQKG

Sequence of entity 2 (E, F, H, I), FASTA

>8UY3_2 Folliculin-interacting protein 1 (chains E, F, H, I)
GRNKSSLLFKESEETRTPNCNCKYCSHPVLG

Sequence of entity 3 (J, K, M), FASTA

>8UY3_3 Mitochondrial import receptor subunit TOM20 homolog (chains J, K, M)
DAEAVQKFFLEEIQLGEELLAQGEYEKGVDHLTNAIAVCGQPQQLLQVLQQTLPPPVFQM
LLTKLP

Ligands and cofactors

ID	Name	Formula	Copies
ZN	Zinc ion	Zn	8
PO4	Phosphate ion	O4 P	1

Water and common crystallization additives (EPE, SO4) are not listed.

Primary citation

Reactive oxygen species control protein degradation at the mitochondrial import gate. McMinimy, R., Manford, A.G., Gee, C.L. et al. Mol Cell (2024) 84:4612-4628.e13. DOI 10.1016/j.molcel.2024.11.004 · PubMed

Other PDB entries of the same protein (UniProt Q9Z2G0 (AlphaFold model), which also has an AlphaFold model), best resolution first:

7ROY 2.9 Å, The structure of the Fem1B:FNIP1 complex

Browse structure collections

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