3N96: Human CRFR2 alpha extracellular domain
Crystal structure of human CRFR2 alpha extracellular domain in complex with Urocortin 1. Determined by X-ray diffraction at 2.75 Å resolution. Released 20 Oct 2010.
- Method
- X-ray diffraction
- Resolution
- 2.75 Å
- Organisms
- Homo sapiens, Homo Sapiens
- Chains
- 8
- Atoms
- 15,249
- Mol. weight
- 221.75 kDa
- Released
- 20 Oct 2010
Explore 3N96 in 3D
Show helices and sheets
RCSB PDB
PDBe
Secondary structure: helices and β-sheets
3N96 contains 120 α-helices and 146 β-strands across 8 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: 28 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--298 | 6 | |
| β-strand | -294 | 1 | 2 |
| α-helix | -293--291 | 3 | |
| α-helix | -287--284 | 4 | |
| β-strand | -281 | 1 | 3 |
| α-helix | -279--274 | 6 | |
| 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 | -239--230 | 10 | |
| β-strand | -225--223 | 3 | 5 |
| α-helix | -216--209 | 8 | |
| 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--132 | 7 | |
| 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--76 | 8 | |
| 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--19 | 16 | |
| α-helix | -13--4 | 10 | |
| α-helix | -2-27 | 30 | |
| α-helix | 30 | 1 | |
| β-strand | 39-40 | 2 | 10 |
| β-strand | 43-44 | 2 | 11 |
| β-strand | 50-51 | 2 | 11 |
| α-helix | 52-53 | 2 | |
| β-strand | 54-55 | 2 | 10 |
| β-strand | 59-63 | 5 | 12 |
| 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 |
| β-strand | 89 | 1 | 15 |
| β-strand | 94 | 1 | 12 |
| β-strand | 100 | 1 | 14 |
Chain B: 30 helices, 37 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--319 | 9 | |
| β-strand | -311--307 | 5 | 16 |
| α-helix | -306--304 | 3 | |
| α-helix | -303--298 | 6 | |
| β-strand | -294 | 1 | 17 |
| α-helix | -293--291 | 3 | |
| 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 | -264--259 | 6 | 16 |
| β-strand | -256--252 | 5 | 20 |
| β-strand | -242 | 1 | 21 |
| α-helix | -239--230 | 10 | |
| β-strand | -225--223 | 3 | 20 |
| α-helix | -216--214 | 3 | |
| α-helix | -212--209 | 4 | |
| 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--132 | 7 | |
| β-strand | -128--125 | 4 | 20 |
| α-helix | -124--122 | 3 | |
| β-strand | -121 | 1 | 21 |
| β-strand | -120 | 1 | 23 |
| β-strand | -117 | 1 | 23 |
| α-helix | -116--115 | 2 | |
| α-helix | -113 | 1 | |
| β-strand | -112--111 | 2 | 24 |
| 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 | 24 |
| α-helix | -40--39 | 2 | |
| α-helix | -34--19 | 16 | |
| α-helix | -13--4 | 10 | |
| α-helix | -2-27 | 30 | |
| α-helix | 30 | 1 | |
| β-strand | 39-40 | 2 | 25 |
| β-strand | 43-44 | 2 | 26 |
| α-helix | 49 | 1 | |
| β-strand | 50-51 | 2 | 26 |
| α-helix | 52-53 | 2 | |
| β-strand | 54-55 | 2 | 25 |
| β-strand | 59-63 | 5 | 27 |
| β-strand | 67-68 | 2 | 28 |
| β-strand | 71-72 | 2 | 28 |
| β-strand | 73 | 1 | 29 |
| β-strand | 78-82 | 5 | 27 |
| β-strand | 83 | 1 | 30 |
| β-strand | 89 | 1 | 30 |
| β-strand | 94 | 1 | 27 |
| β-strand | 100 | 1 | 29 |
Chain C: 29 helices, 36 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | -368--367 | 2 | |
| β-strand | -363--360 | 4 | 31 |
| α-helix | -353--339 | 15 | |
| β-strand | -335--332 | 4 | 31 |
| α-helix | -327--319 | 9 | |
| β-strand | -311--307 | 5 | 31 |
| α-helix | -306--304 | 3 | |
| α-helix | -303--298 | 6 | |
| β-strand | -294--293 | 2 | 31 |
| α-helix | -292--291 | 2 | |
| α-helix | -287--284 | 4 | |
| β-strand | -281 | 1 | 32 |
| α-helix | -279--274 | 6 | |
| β-strand | -272--271 | 2 | 33 |
| β-strand | -268--267 | 2 | 33 |
| β-strand | -264--259 | 6 | 31 |
| β-strand | -256--252 | 5 | 34 |
| β-strand | -242 | 1 | 35 |
| α-helix | -241--239 | 3 | |
| α-helix | -238--229 | 10 | |
| β-strand | -225--223 | 3 | 34 |
| α-helix | -216--209 | 8 | |
| β-strand | -203--198 | 6 | 36 |
| β-strand | -195--188 | 8 | 36 |
| α-helix | -184--170 | 15 | |
| α-helix | -160--152 | 9 | |
| β-strand | -148--143 | 6 | 34 |
| α-helix | -141--139 | 3 | |
| α-helix | -138--132 | 7 | |
| β-strand | -128--125 | 4 | 34 |
| α-helix | -124--122 | 3 | |
| β-strand | -121 | 1 | 35 |
| β-strand | -120 | 1 | 37 |
| β-strand | -117 | 1 | 37 |
| α-helix | -113 | 1 | |
| β-strand | -112--111 | 2 | 38 |
| β-strand | -110--103 | 8 | 31 |
| α-helix | -97--91 | 7 | |
| α-helix | -90--86 | 5 | |
| α-helix | -83--76 | 8 | |
| β-strand | -69--68 | 2 | 31 |
| β-strand | -66 | 1 | 32 |
| α-helix | -65--59 | 7 | |
| α-helix | -55--44 | 12 | |
| β-strand | -42--41 | 2 | 38 |
| α-helix | -40--39 | 2 | |
| α-helix | -34--18 | 17 | |
| α-helix | -13--2 | 12 | |
| α-helix | 1-27 | 27 | |
| β-strand | 39-40 | 2 | 39 |
| α-helix | 41 | 1 | |
| β-strand | 43-44 | 2 | 40 |
| β-strand | 50-51 | 2 | 40 |
| α-helix | 52-53 | 2 | |
| β-strand | 54-55 | 2 | 39 |
| β-strand | 59-63 | 5 | 41 |
| α-helix | 64-65 | 2 | |
| β-strand | 67-68 | 2 | 42 |
| β-strand | 71-72 | 2 | 42 |
| β-strand | 73 | 1 | 43 |
| β-strand | 78-82 | 5 | 41 |
| β-strand | 83 | 1 | 44 |
| β-strand | 89 | 1 | 44 |
| β-strand | 94 | 1 | 41 |
| β-strand | 100 | 1 | 43 |
Chain D: 29 helices, 36 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | -368--367 | 2 | |
| β-strand | -363--360 | 4 | 45 |
| α-helix | -353--339 | 15 | |
| β-strand | -335--332 | 4 | 45 |
| α-helix | -327--319 | 9 | |
| β-strand | -311--307 | 5 | 45 |
| α-helix | -306--304 | 3 | |
| α-helix | -303--298 | 6 | |
| β-strand | -294--293 | 2 | 45 |
| α-helix | -292--291 | 2 | |
| α-helix | -287--284 | 4 | |
| β-strand | -281 | 1 | 46 |
| α-helix | -279--274 | 6 | |
| β-strand | -272--271 | 2 | 47 |
| β-strand | -268--267 | 2 | 47 |
| β-strand | -264--259 | 6 | 45 |
| β-strand | -256--252 | 5 | 48 |
| β-strand | -242 | 1 | 49 |
| α-helix | -241--239 | 3 | |
| α-helix | -238--229 | 10 | |
| β-strand | -225--223 | 3 | 48 |
| α-helix | -216--207 | 10 | |
| β-strand | -203--198 | 6 | 50 |
| β-strand | -195--188 | 8 | 50 |
| α-helix | -184--170 | 15 | |
| α-helix | -160--152 | 9 | |
| β-strand | -148--143 | 6 | 48 |
| α-helix | -141--139 | 3 | |
| α-helix | -138--132 | 7 | |
| β-strand | -128--125 | 4 | 48 |
| α-helix | -124--122 | 3 | |
| β-strand | -121 | 1 | 49 |
| β-strand | -120 | 1 | 51 |
| β-strand | -117 | 1 | 51 |
| α-helix | -113 | 1 | |
| β-strand | -112--111 | 2 | 52 |
| β-strand | -110--103 | 8 | 45 |
| α-helix | -97--91 | 7 | |
| α-helix | -90--86 | 5 | |
| α-helix | -83--76 | 8 | |
| β-strand | -69--68 | 2 | 45 |
| β-strand | -66 | 1 | 46 |
| α-helix | -65--59 | 7 | |
| α-helix | -55--44 | 12 | |
| β-strand | -42--41 | 2 | 52 |
| α-helix | -40--39 | 2 | |
| α-helix | -34--18 | 17 | |
| α-helix | -13--2 | 12 | |
| α-helix | 1-27 | 27 | |
| β-strand | 39-40 | 2 | 53 |
| α-helix | 41 | 1 | |
| β-strand | 43-44 | 2 | 54 |
| α-helix | 49 | 1 | |
| β-strand | 50-51 | 2 | 54 |
| α-helix | 52 | 1 | |
| β-strand | 54-55 | 2 | 53 |
| β-strand | 59-63 | 5 | 55 |
| β-strand | 67-68 | 2 | 56 |
| β-strand | 71-72 | 2 | 56 |
| β-strand | 73 | 1 | 57 |
| β-strand | 78-82 | 5 | 55 |
| β-strand | 83 | 1 | 58 |
| β-strand | 89 | 1 | 58 |
| β-strand | 94 | 1 | 55 |
| β-strand | 100 | 1 | 57 |
Chains E and F: 1 helix, 0 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 27-40 | 14 | |
Chain G: 1 helix, 0 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 31-40 | 10 | |
Chain H: 1 helix, 0 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 34-40 | 7 | |
Molecules and chains
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|
| Maltose binding protein-CRFR2 alpha | A, B, C, D | protein | 482 | Homo sapiens | P0AEX9 (AlphaFold model), Q13324 (AlphaFold model) |
| Urocortin | E, F, G, H | protein | 17 | Homo Sapiens | P55089 (AlphaFold model) |
Sequence of entity 1 (A, B, C, D), FASTA
>3N96_1 Maltose binding protein-CRFR2 alpha (chains A, B, C, D)
MAKIEEGKLVIWINGDKGYNGLAEVGKKFEKDTGIKVTVEHPDKLEEKFPQVAATGDGPD
IIFWAHDRFGGYAQSGLLAEITPDKAFQDKLYPFTWDAVRYNGKLIAYPIAVEALSLIYN
KDLLPNPPKTWEEIPALDKELKAKGKSALMFNLQEPYFTWPLIAADGGYAFKYENGKYDI
KDVGVDNAGAKAGLTFLVDLIKNKHMNADTDYSIAEAAFNKGETAMTINGPWAWSNIDTS
KVNYGVTVLPTFKGQPSKPFVGVLSAGINAASPNKELAKEFLENYLLTDEGLEAVNKDKP
LGAVALKSYEEELAKDPRIAATMENAQKGEIMPNIPQMSAFWYAVRTAVINAASGRQTVD
EALKDAQTNAAAEFAALLHSLLEANCSLALAEELLLDGWGPPLDPEGPYSYCNTTLDQIG
TCWPRSAAGALVERPCPEYFNGVKYNTTRNAYRECLENGTWASKINYSQCEPILDDHHHH
HH
Sequence of entity 2 (E, F, G, H), FASTA
>3N96_2 Urocortin (chains E, F, G, H)
SQRERAEQNRIIFDSVX
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
Browse structure collections
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