7CNG: CDK5R1 bound FEM1B

Structure of CDK5R1 bound FEM1B. Determined by X-ray diffraction at 3.49 Å resolution. Released 21 Oct 2020.

Method: X-ray diffraction
Resolution: 3.49 Å
Organism: Homo sapiens
Chains: 2
Atoms: 5,124
Mol. weight: 78.98 kDa
Released: 21 Oct 2020

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

Secondary structure: helices and β-sheets

7CNG contains 42 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: 20 helices, 4 β-strands

Element	Residues	Length	Sheet
α-helix	2-14	13
α-helix	17-24	8
α-helix	29-35	7
β-strand	40-41	2	1
β-strand	46-47	2	1
α-helix	49-56	8
α-helix	59-67	9
β-strand	76-81	6	2
β-strand	84-90	7	2
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	232-239	8
α-helix	247-258	12
α-helix	269-283	15
α-helix	295-299	5
α-helix	311-315	5
α-helix	321-336	16

Chain B: 22 helices, 4 β-strands

Element	Residues	Length	Sheet
α-helix	1-14	14
α-helix	17-24	8
α-helix	29-35	7
β-strand	40-42	3	3
β-strand	45-47	3	3
α-helix	49-55	7
α-helix	59-63	5
α-helix	64-68	5
β-strand	76-80	5	4
β-strand	85-90	6	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	222-228	7
α-helix	232-239	8
α-helix	248-262	15
α-helix	269-283	15
α-helix	295-299	5
α-helix	300-302	3
α-helix	311-315	5
α-helix	321-335	15

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Protein fem-1 homolog B,Peptide from Cyclin-dependent kinase 5 activator 1	A, B	protein	357	Homo sapiens	Q15078 (AlphaFold model), Q9UK73 (AlphaFold model)

Sequence of entity 1 (A, B), FASTA

>7CNG_1 Protein fem-1 homolog B,Peptide from Cyclin-dependent kinase 5 activator 1 (chains A, B)
GHMEGLAGYVYKAASEGKVLTLAALLLNRSESDIRYLLGYVSQQGGQRSTPLIIAARNGH
AKVVRLLLEHYRVQTQQTGTVRFDGYVIDGATALWCAAGAGHFEVVKLLVSHGANVNHTT
VTNSTPLRAACFDGRLDIVKYLVENNANISIANKYDNTCLMIAAYKGHTDVVRYLLEQRA
DPNAKAHCGATALHFAAEAGHIDIVKELIKWRAAIVVNGHGMTPLKVAAESCKADVVELL
LSHADCDRRSRIEALELLGASFANDRENYDIIKTYHYLYLAMLERFQDGDNILEKEVLPP
IHAYGNRTECRNPQELESIRQDRDALHMEGLIVRERILGGGGSGGGSKKRLLLGLDR

Primary citation

Molecular basis for arginine C-terminal degron recognition by Cul2 FEM1 E3 ligase. Chen, X., Liao, S., Makaros, Y. et al. Nat Chem Biol (2021) 17:254-262. DOI 10.1038/s41589-020-00704-3 · PubMed

Other PDB entries of the same protein (UniProt Q15078 (AlphaFold model), which also has an AlphaFold model), best resolution first:

3O0G 1.95 Å, Crystal Structure of Cdk5:p25 in complex with an ATP analogue
7VDP 2.09 Å, The structure of cyclin-dependent kinase 5 (CDK5) in complex with p25 and Compound 1
1UNL 2.2 Å, Structural mechanism for the inhibition of CD5-p25 from the roscovitine, aloisine and…
1UNG 2.3 Å, Structural mechanism for the inhibition of CDK5-p25 by roscovitine, aloisine and…
1UNH 2.35 Å, Structural mechanism for the inhibition of CDK5-p25 by roscovitine, aloisine and…
6LDP 2.35 Å, Structure of CDK5R1-bound FEM1C
7VDR 2.55 Å, The structure of cyclin-dependent kinase 5 (CDK5) in complex with p25 and Compound 13
1H4L 2.65 Å, Structure and regulation of the CDK5-p25(nck5a) complex
7VDQ 2.91 Å, The structure of cyclin-dependent kinase 5 (CDK5) in complex with p25 and Compound 7
7VDS 3.05 Å, The structure of cyclin-dependent kinase 5 (CDK5) in complex with p25 and Compound 24

Browse structure collections

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