3N93: Human CRFR2 alpha extracellular domain

Crystal structure of human CRFR2 alpha extracellular domain in complex with Urocortin 3. Determined by X-ray diffraction at 2.5 Å resolution. Released 20 Oct 2010.

Method: X-ray diffraction
Resolution: 2.5 Å
Organisms: Homo sapiens, Homo Sapiens
Chains: 3
Atoms: 7,553
Mol. weight: 108.76 kDa
Released: 20 Oct 2010

Explore 3N93 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

3N93 contains 58 α-helices and 73 β-strands across 3 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: 30 helices, 37 β-strands

Element	Residues	Length	Sheet
α-helix	-368--367	2
β-strand	-363--360	4	1
α-helix	-353--339	15
β-strand	-335--332	4	1
α-helix	-327--319	9
β-strand	-311--307	5	1
α-helix	-306--304	3
α-helix	-303--297	7
β-strand	-294	1	2
α-helix	-293--291	3
α-helix	-287--284	4
β-strand	-281	1	3
α-helix	-279--275	5
β-strand	-272--271	2	4
β-strand	-268--267	2	4
β-strand	-264--259	6	1
β-strand	-256--252	5	5
β-strand	-242	1	6
α-helix	-241--239	3
α-helix	-238--230	9
β-strand	-225--223	3	5
α-helix	-216--207	10
β-strand	-203--198	6	7
β-strand	-195--188	8	7
α-helix	-184--170	15
α-helix	-160--152	9
β-strand	-148--143	6	5
α-helix	-141--139	3
α-helix	-138--133	6
β-strand	-128--125	4	5
α-helix	-124--122	3
β-strand	-121	1	6
β-strand	-120	1	8
β-strand	-117	1	8
α-helix	-116--115	2
α-helix	-113	1
β-strand	-112--111	2	9
β-strand	-110--104	7	1
β-strand	-103	1	2
α-helix	-97--91	7
α-helix	-90--86	5
α-helix	-83--74	10
β-strand	-69--68	2	1
β-strand	-66	1	3
α-helix	-65--59	7
α-helix	-55--44	12
β-strand	-42--41	2	9
α-helix	-40--39	2
α-helix	-34--18	17
α-helix	-13--4	10
α-helix	-2-27	30
β-strand	39-40	2	10
α-helix	41-42	2
β-strand	43-44	2	11
β-strand	50-51	2	11
β-strand	54-55	2	10
β-strand	59-63	5	12
α-helix	64-65	2
β-strand	67-68	2	13
β-strand	71-72	2	13
β-strand	73	1	14
β-strand	78-82	5	12
β-strand	83	1	15
α-helix	84	1
β-strand	89	1	15
β-strand	94	1	12
β-strand	100	1	14

Chain B: 27 helices, 36 β-strands

Element	Residues	Length	Sheet
α-helix	-368--367	2
β-strand	-363--360	4	16
α-helix	-353--339	15
β-strand	-335--332	4	16
α-helix	-327--317	11
β-strand	-311--307	5	16
α-helix	-306--304	3
α-helix	-303--298	6
β-strand	-294	1	17
α-helix	-287--284	4
β-strand	-281	1	18
α-helix	-279--274	6
β-strand	-272--271	2	19
β-strand	-268--267	2	19
β-strand	-265--259	7	16
β-strand	-256--252	5	20
β-strand	-242	1	21
α-helix	-241--239	3
α-helix	-238--229	10
β-strand	-225--223	3	20
α-helix	-216--207	10
β-strand	-203--198	6	22
β-strand	-195--188	8	22
α-helix	-184--170	15
α-helix	-160--152	9
β-strand	-148--143	6	20
α-helix	-141--139	3
α-helix	-138--133	6
β-strand	-128--125	4	20
α-helix	-124--122	3
β-strand	-121--120	2	21
β-strand	-117--116	2	21
α-helix	-113	1
β-strand	-112--111	2	23
β-strand	-110--104	7	16
β-strand	-103	1	17
α-helix	-97--91	7
α-helix	-90--86	5
α-helix	-83--76	8
β-strand	-69--68	2	16
β-strand	-66	1	18
α-helix	-65--59	7
α-helix	-55--44	12
β-strand	-42--41	2	23
α-helix	-40--39	2
α-helix	-34--18	17
α-helix	-13--2	12
α-helix	1-24	24
β-strand	39-40	2	24
α-helix	41-42	2
β-strand	43-44	2	25
β-strand	50-51	2	25
β-strand	54-55	2	24
β-strand	59-63	5	26
α-helix	64-65	2
β-strand	67-68	2	27
β-strand	71-72	2	27
β-strand	73	1	28
β-strand	78-82	5	26
β-strand	83	1	29
β-strand	89	1	29
β-strand	94	1	26
β-strand	100	1	28

Chain C: 1 helix, 0 β-strands

Element	Residues	Length	Sheet
α-helix	27-40	14

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Maltose binding protein-CRFR2 alpha	A, B	protein	482	Homo sapiens	P0AEX9 (AlphaFold model), Q13324 (AlphaFold model)
Urocortin-3	C	protein	17	Homo Sapiens	Q969E3 (AlphaFold model)

Sequence of entity 1 (A, B), FASTA

>3N93_1 Maltose binding protein-CRFR2 alpha (chains A, B)
MAKIEEGKLVIWINGDKGYNGLAEVGKKFEKDTGIKVTVEHPDKLEEKFPQVAATGDGPD
IIFWAHDRFGGYAQSGLLAEITPDKAFQDKLYPFTWDAVRYNGKLIAYPIAVEALSLIYN
KDLLPNPPKTWEEIPALDKELKAKGKSALMFNLQEPYFTWPLIAADGGYAFKYENGKYDI
KDVGVDNAGAKAGLTFLVDLIKNKHMNADTDYSIAEAAFNKGETAMTINGPWAWSNIDTS
KVNYGVTVLPTFKGQPSKPFVGVLSAGINAASPNKELAKEFLENYLLTDEGLEAVNKDKP
LGAVALKSYEEELAKDPRIAATMENAQKGEIMPNIPQMSAFWYAVRTAVINAASGRQTVD
EALKDAQTNAAAEFAALLHSLLEANCSLALAEELLLDGWGPPLDPEGPYSYCNTTLDQIG
TCWPRSAAGALVERPCPEYFNGVKYNTTRNAYRECLENGTWASKINYSQCEPILDDHHHH
HH

Sequence of entity 2 (C), FASTA

>3N93_2 Urocortin-3 (chains C)
NLRAQAAANAHLMAQIX

Primary citation

Structural basis of ligand selectivity in human CRFR1 and CRFR2 alpha extracellular domain. Pal, K., Swaminathan, K., Pioszak, A.A. et al. To be published.

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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