1O7F: Regulatory domain of EPAC2

Name: PDB 1O7F: Crystal structure of the regulatory domain of EPAC2
Published: 2002-11-11
License: https://creativecommons.org/publicdomain/zero/1.0/
Keywords: regulation

Crystal structure of the regulatory domain of EPAC2. Determined by X-ray diffraction at 2.5 Å resolution. Released 11 Nov 2002.

Method: X-ray diffraction
Resolution: 2.5 Å
Organism: MUS MUSCULUS
Chains: 1
Atoms: 3,437
Mol. weight: 53.27 kDa
Released: 11 Nov 2002

Explore 1O7F in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

1O7F contains 24 α-helices and 23 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: 24 helices, 23 β-strands

Element	Residues	Length	Sheet
α-helix	14-19	6
α-helix	28-38	11
α-helix	49-58	10
β-strand	60-64	5	1
β-strand	69-71	3	2
β-strand	76	1	3
α-helix	77	1
β-strand	79-85	7	1
β-strand	88-92	5	2
α-helix	98-100	3
β-strand	102-107	6	2
β-strand	112-113	2	1
α-helix	115-119	5
α-helix	121	1
β-strand	122	1	3
α-helix	123	1
β-strand	126-129	4	2
β-strand	133-139	7	1
α-helix	140-150	11
α-helix	151-153	3
α-helix	159	1
α-helix	184-199	16
α-helix	201-203	3
β-strand	205-208	4	4
β-strand	213-217	5	4
β-strand	218-219	2	5
α-helix	220-229	10
α-helix	237-249	13
β-strand	253-255	3	5
β-strand	268-271	4	5
α-helix	272-274	3
α-helix	285-292	8
α-helix	295-313	19
α-helix	323-333	11
α-helix	337-339	3
α-helix	344-353	10
β-strand	355-359	5	2
β-strand	365-367	3	6
β-strand	375-381	7	2
β-strand	383-388	6	6
β-strand	392-398	7	6
β-strand	402-403	2	2
α-helix	405-408	4
α-helix	413-414	2
β-strand	417-420	4	6
β-strand	425-431	7	2
α-helix	432-441	10

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Camp-dependent RAP1 guanine-nucleotide exchange factor	A	protein	469	MUS MUSCULUS	Q9EQZ6 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>1O7F_1 CAMP-DEPENDENT RAP1 GUANINE-NUCLEOTIDE EXCHANGE FACTOR (chains A)
GSPGIPMVAAHAAHSQSSAEWIACLDKRPLERSSEDVDIIFTRLKGVKAFEKFHPNLLRQ
ICLCGYYENLEKGITLFRQGDIGTNWYAVLAGSLDVKVSETSSHQDAVTICTLGIGTAFG
ESILDNTPRHATIVTRESSELLRIEQEDFKALWEKYRQYMAGLLAPPYGVMETGSNNDRI
PDKENVPSEKILRAGKILRIAILSRAPHMIRDRKYHLKTYRQCCVGTELVDWMIQQTSCV
HSRTQAVGMWQVLLEDGVLNHVDQERHFQDKYLFYRFLDDEREDAPLPTEEEKKECDEEL
QDTMLLLSQMGPDAHMRMILRKPPGQRTVDDLEIIYDELLHIKALSHLSTTVKRELAGVL
IFESHAKGGTVLFNQGEEGTSWYIILKGSVNVVIYGKGVVCTLHEGDDFGKLALVNDAPR
AASIVLREDNCHFLRVDKEDFNRILRDVEANTVRLKEHDQDVLVLEKVP

Primary citation

Structure and Regulation of the Camp-Binding Domains of Epac2. Rehmann, H., Prakash, B., Wolf, E. et al. Nat Struct Biol (2002) 10:26. DOI 10.1038/NSB878 · 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
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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