9PQE: Fem-1 homolog B

Name: PDB 9PQE: Fem-1 homolog B (FEM1B) in complex with VU0412674
Published: 2025-11-26
License: https://creativecommons.org/publicdomain/zero/1.0/
Keywords: ligase

Fem-1 homolog B (FEM1B) in complex with VU0412674. Determined by X-ray diffraction at 3.1 Å resolution. Released 26 Nov 2025.

Method: X-ray diffraction
Resolution: 3.1 Å
Organism: Homo sapiens
Chains: 2
Atoms: 5,176
Mol. weight: 79.07 kDa
Ligands: A1CI9
Released: 26 Nov 2025

Explore 9PQE in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

9PQE contains 41 α-helices and 8 β-strands across 2 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: 21 helices, 4 β-strands

Element	Residues	Length	Sheet
α-helix	1-14	14
α-helix	17-23	7
α-helix	29-37	9
β-strand	40-41	2	1
β-strand	46-47	2	1
α-helix	49-56	8
α-helix	59-64	6
α-helix	65-69	5
β-strand	77-81	5	2
β-strand	84-89	6	2
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	190-196	7
α-helix	200-208	9
α-helix	222-228	7
α-helix	232-239	8
α-helix	247-262	16
α-helix	269-283	15
α-helix	295-298	4
α-helix	311-317	7
α-helix	321-336	16

Chain B: 20 helices, 4 β-strands

Element	Residues	Length	Sheet
α-helix	4-13	10
α-helix	17-23	7
α-helix	31-37	7
β-strand	40-41	2	3
β-strand	46-47	2	3
α-helix	49-55	7
α-helix	59-67	9
β-strand	76-81	6	4
β-strand	84-90	7	4
α-helix	91-97	7
α-helix	101-108	8
α-helix	124-131	8
α-helix	134-142	9
α-helix	157-163	7
α-helix	167-175	9
α-helix	190-196	7
α-helix	200-207	8
α-helix	222-228	7
α-helix	232-238	7
α-helix	245-262	18
α-helix	269-282	14
α-helix	295-298	4
α-helix	311-317	7
α-helix	321-335	15

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Protein fem-1 homolog B	A, B	protein	357	Homo sapiens	Q9UK73 (AlphaFold model)

Sequence of entity 1 (A, B), FASTA

>9PQE_1 Protein fem-1 homolog B (chains A, B)
GHMEGLAGYVYKAASEGKVLTLAALLLNRSESDIRYLLGYVSQQGGQRSTPLIIAARNGH
AKVVRLLLEHYRVQTQQTGTVRFDGYVIDGATALWCAAGAGHFEVVKLLVSHGANVNHTT
VTNSTPLRAACFDGRLDIVKYLVENNANISIANKYDNTCLMIAAYKGHTDVVRYLLEQRA
DPNAKAHCGATALHFAAEAGHIDIVKELIKWRAAIVVNGHGMTPLKVAAESCKADVVELL
LSHADCDRRSRIEALELLGASFANDRENYDIIKTYHYLYLAMLERFQDGDNILEKEVLPP
IHAYGNRTECRNPQELESIRQDRDALHMEGLIVRERILGGGGSGGGSKKRLLLGLDR

Ligands and cofactors

ID	Name	Formula	Copies
A1CI9	N-[4-(propan-2-yl)phenyl]pyrazine-2-carboxamide	C14 H15 N3 O	2

Primary citation

Nuclear Magnetic Resonance-based fragment screen of the E3 ligase Fem-1 homolog B. Katinas, J.M., Amporndanai, K., Taylor, A.J. et al. Protein Sci (2025) 34:e70365-e70365. DOI 10.1002/pro.70365 · 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
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…
8WQA 3.39 Å, Cryo-EM structure of CUL2-RBX1-ELOB-ELOC-FEM1B bound with the C-degron of CCDC89…

Browse structure collections

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