3EHU: PDB entry 3EHU

Crystal structure of the extracellular domain of human corticotropin releasing factor receptor type 1 (CRFR1) in complex with CRF. Determined by X-ray diffraction at 1.96 Å resolution. Released 30 Sept 2008.

Method: X-ray diffraction
Resolution: 1.96 Å
Organisms: Escherichia coli, Homo sapiens
Chains: 4
Atoms: 7,584
Mol. weight: 111.23 kDa
Ligands: BTB, CA
Released: 30 Sept 2008

Explore 3EHU in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

3EHU contains 64 α-helices and 67 β-strands across 4 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: 31 helices, 34 β-strands

Element	Residues	Length	Sheet
α-helix	-347--346	2
β-strand	-342--339	4	1
α-helix	-332--318	15
β-strand	-314--311	4	1
α-helix	-306--298	9
β-strand	-290--286	5	1
α-helix	-285--283	3
α-helix	-282--277	6
β-strand	-273	1	2
α-helix	-272--270	3
α-helix	-266--263	4
β-strand	-260	1	3
α-helix	-258--253	6
β-strand	-251--250	2	4
β-strand	-247--246	2	4
β-strand	-243--238	6	1
β-strand	-235--231	5	5
β-strand	-221	1	6
α-helix	-220--218	3
α-helix	-217--209	9
β-strand	-204--202	3	5
α-helix	-191--186	6
β-strand	-182--177	6	7
β-strand	-174--167	8	7
α-helix	-163--149	15
α-helix	-139--131	9
β-strand	-127--122	6	5
α-helix	-120--118	3
α-helix	-117--111	7
β-strand	-107--104	4	5
α-helix	-103--101	3
β-strand	-100	1	6
β-strand	-99	1	8
β-strand	-96	1	8
α-helix	-92	1
β-strand	-91--90	2	9
β-strand	-89--83	7	1
β-strand	-82	1	2
α-helix	-76--71	6
α-helix	-70--65	6
α-helix	-62--53	10
β-strand	-48--47	2	1
β-strand	-45	1	3
α-helix	-44--38	7
β-strand	-21--20	2	9
α-helix	-19--18	2
α-helix	-13-2	16
α-helix	8-19	12
α-helix	28-32	5
β-strand	43-44	2	10
α-helix	45-46	2
β-strand	47-48	2	11
α-helix	53	1
β-strand	54-55	2	11
α-helix	56-57	2
β-strand	58-59	2	10
β-strand	62-67	6	12
α-helix	68-69	2
β-strand	71	1	13
β-strand	76	1	13
β-strand	82-87	6	12
α-helix	92	1
β-strand	93	1	12
α-helix	94	1
β-strand	98	1	12

Chain B: 31 helices, 33 β-strands

Element	Residues	Length	Sheet
α-helix	-347--346	2
β-strand	-342--339	4	14
α-helix	-332--318	15
β-strand	-314--311	4	14
α-helix	-306--298	9
β-strand	-290--286	5	14
α-helix	-285--283	3
α-helix	-282--277	6
β-strand	-273	1	15
α-helix	-272--270	3
α-helix	-266--263	4
β-strand	-260	1	16
α-helix	-258--253	6
β-strand	-251--250	2	17
β-strand	-247--246	2	17
β-strand	-243--238	6	14
β-strand	-235--231	5	18
β-strand	-221	1	19
α-helix	-220--218	3
α-helix	-217--209	9
β-strand	-204--202	3	18
α-helix	-195--193	3
α-helix	-191--186	6
β-strand	-182--177	6	20
β-strand	-174--167	8	20
α-helix	-163--149	15
α-helix	-139--131	9
β-strand	-127--122	6	18
α-helix	-120--115	6
β-strand	-107--104	4	18
α-helix	-103--101	3
β-strand	-100--99	2	19
β-strand	-96--95	2	19
α-helix	-92	1
β-strand	-91--90	2	21
β-strand	-89--83	7	14
β-strand	-82	1	15
α-helix	-76--71	6
α-helix	-70--65	6
α-helix	-62--53	10
β-strand	-48--47	2	14
β-strand	-45	1	16
α-helix	-44--38	7
β-strand	-21--20	2	21
α-helix	-19--18	2
α-helix	-13-3	17
α-helix	8-19	12
α-helix	29-32	4
β-strand	43-44	2	22
α-helix	45-46	2
β-strand	47-48	2	23
α-helix	53	1
β-strand	54-55	2	23
α-helix	56	1
β-strand	58-59	2	22
β-strand	62-67	6	24
α-helix	68-69	2
β-strand	71	1	25
β-strand	76	1	25
β-strand	82-87	6	24
α-helix	92	1
β-strand	93	1	24
α-helix	94	1
β-strand	98	1	24

Chains C and D: 1 helix, 0 β-strands

Element	Residues	Length	Sheet
α-helix	27-40	14

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Fusion protein of CRFR1 extracellular domain and mbp	A, B	protein	476	Escherichia coli, Homo sapiens	P0AEX9 (AlphaFold model), P34998 (AlphaFold model)
Corticoliberin	C, D	protein	21		P06850 (AlphaFold model)

Sequence of entity 1 (A, B), FASTA

>3EHU_1 FUSION PROTEIN OF CRFR1 EXTRACELLULAR DOMAIN AND MBP (chains A, B)
MAKIEEGKLVIWINGDKGYNGLAEVGKKFEKDTGIKVTVEHPDKLEEKFPQVAATGDGPD
IIFWAHDRFGGYAQSGLLAEITPDKAFQDKLYPFTWDAVRYNGKLIAYPIAVEALSLIYN
KDLLPNPPKTWEEIPALDKELKAKGKSALMFNLQEPYFTWPLIAADGGYAFKYENGKYDI
KDVGVDNAGAKAGLTFLVDLIKNKHMNADTDYSIAEAAFNKGETAMTINGPWAWSNIDTS
KVNYGVTVLPTFKGQPSKPFVGVLSAGINAASPNKELAKEFLENYLLTDEGLEAVNKDKP
LGAVALKSYEEELAKDPRIAATMENEQKGEIMPNIPQMSAFWYAVRTAVINAASGRQTVD
EALKDAQTNAAAEFSLQDQHCESLSLASNISGLQCNASVDLIGTCWPRSPAGQLVVRPCP
AFFYGVRYNTTNNGYRECLANGSWAARVNYSECQEILNEEKKSKVHYHVAHHHHHH

Sequence of entity 2 (C, D), FASTA

>3EHU_2 Corticoliberin (chains C, D)
ARAEQLAQQAHSNRKLMEIIX

Ligands and cofactors

ID	Name	Formula	Copies
BTB	2-[bis-(2-hydroxy-ethyl)-amino]-2-hydroxymethyl-propane-1,3-diol	C8 H19 N O5	2
CA	Calcium ion	Ca	2

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

Primary citation

Molecular Recognition of Corticotropin-releasing Factor by Its G-protein-coupled Receptor CRFR1. Pioszak, A.A., Parker, N.R., Suino-Powell, K. et al. J Biol Chem (2008) 283:32900-32912. DOI 10.1074/jbc.M805749200 · PubMed

Other PDB entries of the same protein (UniProt P0AEX9 (AlphaFold model), which also has an AlphaFold model), best resolution first:

8C8F 1.15 Å, Crystal structure of the E. coli maltodextrin-binding protein
4EXK 1.28 Å, A chimera protein containing MBP fused to the C-terminal domain of the uncharacterized…
3Q27 1.3 Å, Cyrstal structure of human alpha-synuclein (32-57) fused to maltose binding protein (MBP)
7KD4 1.31 Å, Structure of the C-terminal domain of the Menangle virus phosphoprotein (residues 329…
5M13 1.37 Å, Synthetic nanobody in complex with MBP
5HZ7 1.43 Å, High-resolution crystal structure of the minor DNA-binding pilin ComP from Neisseria…
5H7Q 1.45 Å, Crystal structure of human MNDA PYD domain with MBP tag
6XDS 1.47 Å, Crystal structure of MBP-TREM2 Ig domain fusion with fragment,…
4IRL 1.47 Å, X-ray structure of the CARD domain of zebrafish GBP-NLRP1 like protein
8SVY 1.47 Å, MBP-Mcl1 in complex with ligand 10
3MP6 1.48 Å, Complex Structure of Sgf29 and dimethylated H3K4
9CLC 1.48 Å, Crystal structure of maltose binding protein (Apo), mutant Trp10 to 4-Cyanotryptophan

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