5MWP: Mineralocorticoid receptor

The structure of MR in complex with AZD9977. Determined by X-ray diffraction at 1.82 Å resolution. Released 7 Mar 2018.

Method: X-ray diffraction
Resolution: 1.82 Å
Organism: Homo sapiens
Chains: 2
Atoms: 2,296
Mol. weight: 36.93 kDa
Ligands: ECV
Released: 7 Mar 2018

Explore 5MWP in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

5MWP contains 12 α-helices and 4 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: 11 helices, 4 β-strands

Element	Residues	Length	Sheet
α-helix	738-744	7
α-helix	746-749	4
α-helix	762-785	24
α-helix	790-792	3
α-helix	795-822	28
β-strand	827-830	4	1
β-strand	833-835	3	1
α-helix	837-842	6
α-helix	846-862	17
α-helix	866-877	12
β-strand	880-882	3	2
α-helix	889-907	19
α-helix	918-947	30
α-helix	958-972	15
β-strand	976-978	3	2

Chain B: 1 helix, 0 β-strands

Element	Residues	Length	Sheet
α-helix	1434-1440	7

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Mineralocorticoid receptor	A	protein	305	Homo sapiens	P08235 (AlphaFold model)
NCOA1 peptide	B	protein	15	Homo sapiens	Q15788 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>5MWP_1 Mineralocorticoid receptor (chains A)
MHNHNHNHNHNHNGGENLYFQGTPSPVMVLENIEPEIVYAGYDSSKPDTAENLLSTLNRL
AGKQMIQVVKWAKVLPGFKNLPLEDQITLIQYSWMSLSSFALSWRSYKHTNSQFLYFAPD
LVFNEEKMHQSAMYELCQGMHQISLQFVRLQLTFEEYTIMKVLLLLSTIPKDGLKSQAAF
EEMRTNYIKELRKMVTKSPNNSGQSWQRFYQLTKLLDSMHDLVSDLLEFCFYTFRESHAL
KVEFPAMLVEIISDQLPKVESGNAKPLYFHRKGGSLVPRGSGGGSGGSGGPQAQQKSLLQ
QLLTE

Sequence of entity 2 (B), FASTA

>5MWP_2 NCOA1 peptide (chains B)
PQAQQKSLLQQLLTE

Ligands and cofactors

ID	Name	Formula	Copies
ECV	2-[(3~{S})-7-fluoranyl-4-[(3-oxidanylidene-4~{H}-1,4-benzoxazin-6-yl)carbonyl]-…	C20 H18 F N3 O5	1

Primary citation

Preclinical pharmacology of AZD9977: A novel mineralocorticoid receptor modulator separating organ protection from effects on electrolyte excretion. Bamberg, K., Johansson, U., Edman, K. et al. PLoS One (2018) 13:e0193380-e0193380. DOI 10.1371/journal.pone.0193380 · PubMed

Other PDB entries of the same protein (UniProt P08235 (AlphaFold model), which also has an AlphaFold model), best resolution first:

4PF3 1.1 Å, Mineralocorticoid receptor ligand-binding domain with compuond 37a
3VHV 1.35 Å, Mineralocorticoid receptor ligand-binding domain with non-steroidal antagonist
3WFG 1.4 Å, Mineralocorticoid receptor ligand-binding domain with compuond 2e
9GC7 1.46 Å, Mineralocorticoid receptor in complex with acylurea antagonists.
6GEV 1.54 Å, Mineralocorticoid receptor in complex with (s)-13
6GGG 1.71 Å, Mineralocorticoid receptor in complex with (s)-13
2AAX 1.75 Å, Mineralocorticoid Receptor Double Mutant with Bound Cortisone
5MWY 1.75 Å, The structure of MR in complex with eplerenone.
6GG8 1.8 Å, Mineralocorticoid receptor in complex with (s)-13
5L7H 1.84 Å, MCR IN COMPLEX WITH ligand
2AB2 1.85 Å, Mineralocorticoid Receptor Double Mutant with Bound Spironolactone
5L7E 1.86 Å, MCR IN COMPLEX WITH ligand

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