4MH0: Selective activation of Epac1 and Epac2

Selective activation of Epac1 and Epac2. Determined by X-ray diffraction at 2.4 Å resolution. Released 3 Sept 2014.

Method: X-ray diffraction
Resolution: 2.4 Å
Organisms: Mus musculus, Homo sapiens
Chains: 2
Atoms: 6,534
Mol. weight: 99.37 kDa
Ligands: HR4
Released: 3 Sept 2014

Explore 4MH0 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

4MH0 contains 42 α-helices and 30 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 E: 36 helices, 22 β-strands

Element	Residues	Length	Sheet
α-helix	311-315	5
α-helix	318-320	3
α-helix	323-333	11
α-helix	344-350	7
α-helix	354	1
β-strand	355-359	5	1
β-strand	365-367	3	2
β-strand	375-381	7	1
β-strand	384-388	5	2
β-strand	392-397	6	2
β-strand	402-403	2	1
α-helix	405-410	6
β-strand	417-420	4	2
β-strand	425-431	7	1
α-helix	432-438	7
β-strand	447-451	5	3
β-strand	454-461	8	3
α-helix	479	1
β-strand	480-485	6	3
α-helix	487-496	10
α-helix	502-504	3
α-helix	505-522	18
α-helix	525-536	12
α-helix	545-570	26
α-helix	571-576	6
α-helix	578-598	21
α-helix	604-611	8
α-helix	644-647	4
β-strand	651-657	7	4
β-strand	663-669	7	4
β-strand	673	1	5
α-helix	674-685	12
β-strand	692-696	5	4
β-strand	702-704	3	4
α-helix	705-706	2
β-strand	710	1	5
β-strand	721-725	5	4
α-helix	727-732	6
α-helix	737-739	3
α-helix	747-750	4
α-helix	755-771	17
α-helix	775-783	9
α-helix	785-787	3
α-helix	793-814	22
α-helix	819-838	20
β-strand	841	1	6
α-helix	842-853	12
α-helix	855-858	4
α-helix	861-866	6
α-helix	869-880	12
α-helix	885-897	13
β-strand	903	1	6
α-helix	906-919	14
β-strand	923-924	2	3
β-strand	927-929	3	3
α-helix	930-946	17
α-helix	963-969	7
α-helix	978-988	11

Chain R: 6 helices, 8 β-strands

Element	Residues	Length	Sheet
β-strand	4-9	6	7
α-helix	16-24	9
β-strand	41-43	3	7
β-strand	52-57	6	7
α-helix	65-74	10
β-strand	77-83	7	7
α-helix	87-91	5
α-helix	93-103	11
β-strand	111-116	6	7
α-helix	129-133	5
β-strand	143-144	2	7
β-strand	147	1	8
β-strand	152	1	8
α-helix	154-163	10

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Rap guanine nucleotide exchange factor 4	E	protein	694	Mus musculus	Q9EQZ6 (AlphaFold model)
Ras-related protein Rap-1b	R	protein	167	Homo sapiens	P61224 (AlphaFold model)

Sequence of entity 1 (E), FASTA

>4MH0_1 Rap guanine nucleotide exchange factor 4 (chains E)
GSPESFPDAHMRMILRKPPGQRTVDDLEIIYDELLHIKALSHLSTTVKRELAGVLIFESH
AKGGTVLFNQGEEGTSWYIILKGSVNVVIYGKGVVCTLHEGDDFGKLALVNDAPRAASIV
LREDNCHFLRVDKEDFNRILRDVEANTVRLKEHDQDVLVLEKVPAGNRAANQGNSQPQQK
YTVMSGTPEKILEHFLETIRLEPSLNEATDSVLNDFVMMHCVFMPNTQLCPALVAHYHAQ
PSQGTEQERMDYALNNKRRVIRLVLQWAAMYGDLLQEDDVAMAFLEEFYVSVSDDARMMA
AFKEQLPELEKIVKQISEDAKAPQKKHKVLLQQFNTGDERAQKRQPIRGSDEVLFKVYCI
DHTYTTIRVPVAASVKEVISAVADKLGSGEGLIIVKMNSGGEKVVLKSNDVSVFTTLTIN
GRLFACPREQFDSLTPLPEQEGPTTGTVGTFELMSSKDLAYQMTTYDWELFNCVHELELI
YHTFGRHNFKKTTANLDLFLRRFNEIQFWVVTEVCLCSQLSKRVQLLKKFIKIAAHCKEY
KNLNSFFAIVMGLSNVAVSRLALTWEKLPSKFKKFYAEFESLMDPSRNHRAYRLTAAKLE
PPLIPFMPLLIKDMTFTHEGNKTFIDNLVNFEKMRMIANTARTVRYYRSQPFNPDAAQAN
KNHQDVRSYVRQLNVIDNQRTLSQMSHRLEPRRP

Sequence of entity 2 (R), FASTA

>4MH0_2 Ras-related protein Rap-1b (chains R)
MREYKLVVLGSGGVGKSALTVQFVQGIFVEKYDPTIEDSYRKQVEVDAQQCMLEILDTAG
TEQFTAMRDLYMKNGQGFALVYSITAQSTFNDLQDLREQILRVKDTDDVPMILVGNKCDL
EDERVVGKEQGQNLARQWNNCAFLESSAKSKINVNEIFYDLVRQINR

Ligands and cofactors

ID	Name	Formula	Copies
HR4	(2S,4aR,6R,7R,7aS)-6-{6-amino-8-[(4-fluorobenzyl)sulfanyl]-9H-purin-9-yl}-2-sul…	C17 H17 F N5 O5 P S2	2

Water and common crystallization additives (SO4) are not listed.

Primary citation

Selective activation of Epac1 and Epac2. Rehmann, H. To be published.

Other PDB entries of the same protein (UniProt Q9EQZ6 (AlphaFold model), which also has an AlphaFold model), best resolution first:

1O7F 2.5 Å, Crystal structure of the regulatory domain of EPAC2
4F7Z 2.6 Å, Conformational dynamics of exchange protein directly activated by cAMP
4MGY 2.6 Å, Selective activation of Epac1 and Epac2
2BYV 2.7 Å, Structure of the cAMP responsive exchange factor Epac2 in its auto- inhibited state
4MGK 2.7 Å, Selective activation of Epac1 and Epac2
4MGI 2.8 Å, Selective activation of Epac1 and Epac2
4MGZ 3.0 Å, Selective activation of Epac1 and Epac2

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