6MOI: Dimeric DARPin C_angle_R5 complex with EpoR

Dimeric DARPin C_angle_R5 complex with EpoR. Determined by X-ray diffraction at 2.06 Å resolution. Released 5 Jun 2019.

Method: X-ray diffraction
Resolution: 2.06 Å
Organisms: synthetic construct, Homo sapiens
Chains: 2
Atoms: 3,390
Mol. weight: 50.79 kDa
Ligands: MG
Released: 5 Jun 2019

Explore 6MOI in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

6MOI contains 23 α-helices and 18 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: 14 helices, 0 β-strands

Element	Residues	Length
α-helix	3-14	12
α-helix	18-26	9
α-helix	41-48	8
α-helix	51-59	9
α-helix	74-81	8
α-helix	84-92	9
α-helix	107-114	8
α-helix	117-125	9
α-helix	140-146	7
α-helix	150-158	9
α-helix	173-179	7
α-helix	183-191	9
α-helix	206-213	8
α-helix	216-221	6

Chain B: 9 helices, 18 β-strands

Element	Residues	Length	Sheet
α-helix	10-21	12
β-strand	27-29	3	1
β-strand	30	1	2
β-strand	36-42	7	1
β-strand	53-59	7	3
β-strand	65-67	3	3
β-strand	70-74	5	1
β-strand	78-85	8	1
α-helix	87-89	3
β-strand	95-102	8	3
β-strand	107-114	8	3
α-helix	115-117	3
β-strand	119	1	2
α-helix	121-124	4
β-strand	125-131	7	4
β-strand	138-143	6	4
α-helix	144	1
α-helix	151-153	3
β-strand	154-162	9	5
β-strand	167-174	8	5
β-strand	180-183	4	4
α-helix	186-187	2
β-strand	191-200	10	5
α-helix	201	1
β-strand	207	1	2
α-helix	209-215	7
β-strand	216-219	4	5

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Dimeric DARPing CCR5 (C_angle_R5)	A	protein	231	synthetic construct
Erythropoietin receptor	B	protein	229	Homo sapiens	P19235 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>6MOI_1 Dimeric DARPing CCR5 (C_angle_R5) (chains A)
MGHHHHHHSDLGKKLLKAARAGQDDEVRILMANGADVNATDIWDATPLHLAALIGHLEIV
EVLLKNGADVNASDITGTTPLHLAATMGHKEIVEVLLKYGADVNAYDLNGATPLHLAARM
GHAEIVAVLLEYGADVNAQDAAGMTPLHLAAANGHDEIVLILLLKGADVNAKDAAGMTPL
HLAAANGHKRIVLVLILAGADVNAQDKFGKTAFDISIDNGNEDLAKILQKQ

Sequence of entity 2 (B), FASTA

>6MOI_2 Erythropoietin receptor (chains B)
FAGSADPKFESKAALLAARGPEELLCFTERLEDLVCFWEEAASAGVGPGQYSFSYQLEDE
PWKLCRLHQAPTARGAVRFWCSLPTADTSSFVPLELRVTAASGAPRYHRVIHINEVVLLD
APVGLVARLADESGHVVLRWLPPPETPMTSHIRYEVDVSAGQGAGSVQRVEILEGRTECV
LSNLRGRTRYTFAVRARMAEPSFGGFWSAWSEPVSLLTPSDLDKEKAAA

Ligands and cofactors

ID	Name	Formula	Copies
MG	Magnesium ion	Mg	2

Water and common crystallization additives (PG4, PGE, PEG, EDO, SO4) are not listed.

Primary citation

Topological control of cytokine receptor signaling induces differential effects in hematopoiesis. Mohan, K., Ueda, G., Kim, A.R. et al. Science (2019) 364. DOI 10.1126/science.aav7532 · PubMed

Other PDB entries of the same protein (UniProt P19235 (AlphaFold model), which also has an AlphaFold model), best resolution first:

1EER 1.9 Å, Crystal structure of human erythropoietin complexed to its receptor at 1.9 Å
6MOE 2.09 Å, Monomeric DARPin E2 complex with EpoR
8VUI 2.1 Å, Structure of FabS1CE-EPR-1, an elbow-locked Fab, in complex with the erythropoeitin…
1ERN 2.4 Å, Native structure of the extracellular domain of erythropoietin (EPO) receptor [ebp]
6MOJ 2.43 Å, Dimeric DARPin A_angle_R5 complex with EpoR
4Y5V 2.6 Å, Diabody 305 complex with EpoR
6E2Q 2.65 Å, Structure of human JAK2 FERM/SH2 in complex with Erythropoietin Receptor
1EBA 2.7 Å, Complex between the extracellular domain of erythropoietin (EPO) receptor [ebp] and an…
1CN4 2.8 Å, Erythropoietin complexed with extracellular domains of erythropoietin receptor
1EBP 2.8 Å, Complex between the extracellular domain of erythropoietin (EPO) receptor [ebp] and an…
4Y5Y 2.85 Å, Diabody 330 complex with EpoR
6MOF 2.89 Å, Monomeric DARPin G2 complex with EpoR

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