7ROY: Fem1B:FNIP1 complex

The structure of the Fem1B:FNIP1 complex. Determined by X-ray diffraction at 2.9 Å resolution. Released 13 Oct 2021.

Method: X-ray diffraction
Resolution: 2.9 Å
Organism: Mus musculus
Chains: 6
Atoms: 12,189
Mol. weight: 177.94 kDa
Ligands: ZN
Released: 13 Oct 2021

Explore 7ROY in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

7ROY contains 100 α-helices and 16 β-strands across 5 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: 23 helices, 4 β-strands

Element	Residues	Length	Sheet
α-helix	0-13	14
α-helix	17-24	8
α-helix	29-36	8
β-strand	40-42	3	1
β-strand	45-47	3	1
α-helix	49-56	8
α-helix	59-69	11
β-strand	76-81	6	1
β-strand	84-90	7	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	190-196	7
α-helix	200-208	9
α-helix	211-213	3
α-helix	222-228	7
α-helix	232-239	8
α-helix	246-259	14
α-helix	269-283	15
α-helix	295-298	4
α-helix	311-316	6
α-helix	321-336	16
α-helix	345-356	12
α-helix	360-372	13

Chain B: 23 helices, 4 β-strands

Element	Residues	Length	Sheet
α-helix	4-13	10
α-helix	17-23	7
α-helix	29-37	9
β-strand	40-42	3	2
β-strand	45-47	3	2
α-helix	49-56	8
α-helix	59-67	9
β-strand	76-81	6	3
β-strand	84-90	7	3
α-helix	91-97	7
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	232-238	7
α-helix	246-259	14
α-helix	269-283	15
α-helix	295-298	4
α-helix	311-316	6
α-helix	321-335	15
α-helix	341-343	3
α-helix	344-356	13
α-helix	360-374	15

Chain C: 24 helices, 4 β-strands

Element	Residues	Length	Sheet
α-helix	0-13	14
α-helix	17-24	8
α-helix	29-37	9
β-strand	40-42	3	4
β-strand	45-47	3	4
α-helix	49-56	8
α-helix	59-69	11
β-strand	76-81	6	4
β-strand	84-90	7	4
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	211-213	3
α-helix	222-228	7
α-helix	232-240	9
α-helix	246-259	14
α-helix	269-283	15
α-helix	295-298	4
α-helix	300-302	3
α-helix	311-316	6
α-helix	321-336	16
α-helix	344-356	13
α-helix	360-376	17

Chain D: 28 helices, 4 β-strands

Element	Residues	Length	Sheet
α-helix	4-13	10
α-helix	17-23	7
α-helix	29-37	9
β-strand	40-42	3	5
β-strand	45-47	3	5
α-helix	49-56	8
α-helix	59-63	5
α-helix	64-68	5
β-strand	77-80	4	6
β-strand	85-89	5	6
α-helix	91-98	8
α-helix	101-109	9
α-helix	124-131	8
α-helix	134-141	8
α-helix	157-164	8
α-helix	167-175	9
α-helix	190-197	8
α-helix	200-208	9
α-helix	211-213	3
α-helix	222-228	7
α-helix	232-238	7
α-helix	246-259	14
α-helix	264-266	3
α-helix	269-283	15
α-helix	295-298	4
α-helix	300-302	3
α-helix	305-308	4
α-helix	311-317	7
α-helix	321-336	16
α-helix	341-343	3
α-helix	344-356	13
α-helix	360-373	14

Chain H: 2 helices, 0 β-strands

Element	Residues	Length	Sheet
α-helix	575-577	3
α-helix	588-590	3

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	G, H	protein	31	Mus musculus	Q68FD7 (AlphaFold model)

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

>7ROY_1 Protein fem-1 homolog B (chains A, B, C, D)
SGSSMEGLAGYVYKAASEGKVLTLAALLLNRSESDIRYLLGYVSQQGGQRSTPLIIAARN
GHAKVVRLLLEHYRVQTQQTGTVRFDGYVIDGATALWCAAGAGHFEVVKLLVSHGANVNH
TTVTNSTPLRAACFDGRLDIVKYLVENNANISIANKYDNTCLMIAAYKGHTDVVRYLLEQ
RADPNAKAHCGATALHFAAEAGHIDIVKELIKWRAAIVVNGHGMTPLKVAAESCKADVVE
LLLSHADCDRRSRIEALELLGASFANDRENYDIMKTYHYLYLAMLERFQDGDNILEKEVL
PPIHAYGNRTECRNPQELEAIRQDRDALHMEGLIVRERILGADNIDVSHPIIYRGAVYAD
NMEFEQCIKLWLHALHLRQKG

Sequence of entity 2 (G, H), FASTA

>7ROY_2 Folliculin-interacting protein 1 (chains G, H)
GRNKSSLLFKESEETRTPNCNCKYCSHPVLG

Ligands and cofactors

ID	Name	Formula	Copies
ZN	Zinc ion	Zn	8

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

Primary citation

Structural basis and regulation of the reductive stress response. Manford, A.G., Mena, E.L., Shih, K.Y. et al. Cell (2021) 184:5375-5390.e16. DOI 10.1016/j.cell.2021.09.002 · PubMed

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

8UY3 3.2 Å, Fem1B with FNIP1 and Tom20 fragment

Browse structure collections

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