4F7Z: Rap guanine nucleotide exchange factor 4

Conformational dynamics of exchange protein directly activated by cAMP. Determined by X-ray diffraction at 2.6 Å resolution. Released 3 Oct 2012.

Method: X-ray diffraction
Resolution: 2.6 Å
Organism: Mus musculus
Chains: 1
Atoms: 7,666
Mol. weight: 114.71 kDa
Released: 3 Oct 2012

Explore 4F7Z in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

4F7Z contains 53 α-helices and 38 β-strands across 1 chain. 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: 53 helices, 38 β-strands

Element	Residues	Length	Sheet
α-helix	15-20	6
α-helix	28-38	11
α-helix	49-58	10
β-strand	60-64	5	1
α-helix	65	1
β-strand	69-71	3	2
α-helix	76-77	2
β-strand	79-85	7	1
β-strand	87-92	6	2
β-strand	102-108	7	2
β-strand	112-113	2	1
α-helix	115-119	5
α-helix	121-123	3
β-strand	126-129	4	2
β-strand	133-139	7	1
α-helix	140-154	15
α-helix	159	1
α-helix	183-199	17
α-helix	201-203	3
β-strand	205-209	5	3
β-strand	212-217	6	3
β-strand	218-219	2	4
α-helix	220-230	11
α-helix	237-249	13
β-strand	253-255	3	4
β-strand	268-271	4	4
α-helix	272-275	4
α-helix	280-283	4
α-helix	284-291	8
α-helix	294-314	21
α-helix	318-320	3
α-helix	323-333	11
α-helix	337-339	3
α-helix	344-350	7
α-helix	354	1
β-strand	355-359	5	2
β-strand	365-367	3	5
β-strand	372	1	6
β-strand	375-381	7	2
β-strand	383-388	6	5
β-strand	392-398	7	5
β-strand	402-403	2	2
α-helix	405-408	4
α-helix	412	1
β-strand	413	1	6
α-helix	414	1
β-strand	417-420	4	5
β-strand	425-431	7	2
α-helix	432-444	13
β-strand	446-450	5	7
β-strand	455-460	6	7
β-strand	481-485	5	7
α-helix	487-497	11
α-helix	505-522	18
α-helix	525-537	13
α-helix	545-570	26
α-helix	571-576	6
α-helix	578-593	16
α-helix	599-602	4
α-helix	604-614	11
β-strand	624-625	2	8
α-helix	641-643	3
β-strand	651-657	7	8
β-strand	663-669	7	8
β-strand	673	1	9
α-helix	674-685	12
β-strand	691-696	6	8
β-strand	702-704	3	8
α-helix	705-706	2
β-strand	710	1	9
β-strand	721-726	6	8
α-helix	727-729	3
α-helix	747-750	4
α-helix	755-771	17
α-helix	775-783	9
α-helix	785-788	4
α-helix	793-814	22
α-helix	819-838	20
β-strand	841	1	10
α-helix	842-851	10
α-helix	855-858	4
α-helix	861-865	5
α-helix	869-880	12
α-helix	885-896	12
β-strand	903	1	10
α-helix	906-918	13
β-strand	923	1	7
β-strand	928-929	2	7
α-helix	930-946	17
α-helix	963-970	8
α-helix	978-986	9

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Rap guanine nucleotide exchange factor 4	A	protein	999	Mus musculus	Q9EQZ6 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>4F7Z_1 Rap guanine nucleotide exchange factor 4 (chains A)
GSPGIPMVAAHAAHSQSSAEWIACLDKRPLERSSEDVDIIFTRLKGVKAFEKFHPNLLRQ
ICLCGYYENLEKGITLFRQGDIGTNWYAVLAGSLDVKVSETSSHQDAVTICTLGIGTAFG
ESILDNTPRHATIVTRESSELLRIEQEDFKALWEKYRQYMAGLLAPPYGVMETGSNNDRI
PDKENVPSEKILRAGKILRIAILSRAPHMIRDRKYHLKTYRQCCVGTELVDWMIQQTSCV
HSRTQAVGMWQVLLEDGVLNHVDQERHFQDKYLFYRFLDDEREDAPLPTEEEKKECDEEL
QDTMLLLSQMGPDAHMRMILRKPPGQRTVDDLEIIYDELLHIKALSHLSTTVKRELAGVL
IFESHAKGGTVLFNQGEEGTSWYIILKGSVNVVIYGKGVVCTLHEGDDFGKLALVNDAPR
AASIVLREDNCHFLRVDKEDGNRILRDVEANTVRLKEHDQDVLVLEKVPAGNRAANQGNS
QPQQKYTVMSGTPEKILEHFLETIRLEPSLNEATDSVLNDFVMMHCVFMPNTQLCPALVA
HYHAQPSQGTEQERMDYALNNKRRVIRLVLQWAAMYGDLLQEDDVAMAFLEEFYVSVSDD
ARMMAAFKEQLPELEKIVKQISEDAKAPQKKHKVLLQQFNTGDERAQKRQPIRGSDEVLF
KVYCIDHTYTTIRVPVAASVKEVISAVADKLGSGEGLIIVKMNSGGEKVVLKSNDVSVFT
TLTINGRLFACPREQFDSLTPLPEQEGPTTGTVGTFELMSSKDLAYQMTTYDWELFNCVH
ELELIYHTFGRHNFKKTTANLDLFLRRFNEIQFWVVTEVCLCSQLSKRVQLLKKFIKIAA
HCKEYKNLNSFFAIVMGLSNVAVSRLALTWEKLPSKFKKFYAEFESLMDPSRNHRAYRLT
AAKLEPPLIPFMPLLIKDMTFTHEGNKTFIDNLVNFEKMRMIANTARTVRYYRSQPFNPD
AAQANKNHQDVRSYVRQLNVIDNQRTLSQMSHRLEPRRP

Primary citation

Structural analyses of a constitutively active mutant of exchange protein directly activated by cAMP. White, M.A., Li, S., Tsalkova, T. et al. PLoS One (2012) 7:e49932-e49932. DOI 10.1371/journal.pone.0049932 · PubMed

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

4MH0 2.4 Å, Selective activation of Epac1 and Epac2
1O7F 2.5 Å, Crystal structure of the regulatory domain of EPAC2
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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