2A3I: Mineralocorticoid receptor

Structural and Biochemical Mechanisms for the Specificity of Hormone Binding and Coactivator Assembly by Mineralocorticoid Receptor. Determined by X-ray diffraction at 1.95 Å resolution. Released 19 Jul 2005.

Method: X-ray diffraction
Resolution: 1.95 Å
Organism: Homo sapiens
Chains: 2
Atoms: 2,349
Mol. weight: 31.24 kDa
Ligands: C0R
Released: 19 Jul 2005

Explore 2A3I in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

2A3I contains 13 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: 12 helices, 4 β-strands

Element	Residues	Length	Sheet
α-helix	738-745	8
α-helix	746-748	3
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	889-909	21
α-helix	915-947	33
α-helix	949-952	4
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	253	Homo sapiens	P08235 (AlphaFold model)
Nuclear receptor coactivator 1, residues 1430-1441	B	protein	12		Q15788 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>2A3I_1 Mineralocorticoid receptor (chains A)
RALTPSPVMVLENIEPEIVYAGYDSSKPDTAENLLSTLNRLAGKQMIQVVKWAKVLPGFK
NLPLEDQITLIQYSWMSLSSFALSWRSYKHTNSQFLYFAPDLVFNEEKMHQSAMYELCQG
MHQISLQFVRLQLTFEEYTIMKVLLLLSTIPKDGLKSQAAFEEMRTNYIKELRKMVTKCP
NNSGQSWQRFYQLTKLLDSMHDLVSDLLEFCFYTFRESHALKVEFPAMLVEIISDQLPKV
ESGNAKPLYFHRK

Sequence of entity 2 (B), FASTA

>2A3I_2 Nuclear receptor coactivator 1, residues 1430-1441 (chains B)
QQKSLLQQLLTE

Ligands and cofactors

ID	Name	Formula	Copies
C0R	Corticosterone	C21 H30 O4	1

Primary citation

Structural and biochemical mechanisms for the specificity of hormone binding and coactivator assembly by mineralocorticoid receptor. Li, Y., Suino, K., Daugherty, J. et al. Mol Cell (2005) 19:367-380. DOI 10.1016/j.molcel.2005.06.026 · 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
5MWP 1.82 Å, The structure of MR in complex with AZD9977.
5L7H 1.84 Å, MCR IN COMPLEX WITH ligand
2AB2 1.85 Å, Mineralocorticoid Receptor Double Mutant with Bound Spironolactone

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