4RWF: PDB entry 4RWF

Crystal structure of the CLR:RAMP2 extracellular domain heterodimer with bound adrenomedullin. Determined by X-ray diffraction at 1.76 Å resolution. Released 20 May 2015.

Method
X-ray diffraction
Resolution
1.76 Å
Organisms
Escherichia coli, Homo sapiens
Chains
2
Atoms
5,009
Mol. weight
70.21 kDa
Released
20 May 2015

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

Secondary structure: helices and β-sheets

4RWF contains 32 α-helices and 38 β-strands across 2 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, 37 β-strands

ElementResiduesLengthSheet
α-helix4-52
β-strand9-1241
α-helix19-3315
β-strand37-4041
α-helix45-5410
β-strand61-6551
α-helix66-683
α-helix69-746
β-strand7812
α-helix79-813
α-helix85-884
β-strand9113
α-helix93-986
β-strand100-10124
β-strand104-10524
β-strand108-11361
β-strand116-12055
β-strand13016
α-helix134-1429
β-strand147-14935
α-helix156-16510
β-strand16917
β-strand173-17428
β-strand177-17828
β-strand18417
α-helix188-20215
α-helix212-2209
β-strand224-22965
α-helix231-2333
α-helix234-2407
β-strand244-24745
α-helix248-2503
β-strand25116
β-strand25219
β-strand25519
α-helix2591
β-strand260-261210
β-strand262-26871
β-strand26912
α-helix275-2806
α-helix281-2866
α-helix289-29810
β-strand303-30421
β-strand30613
α-helix307-3137
α-helix317-32812
β-strand330-331210
α-helix332-3332
α-helix338-35316
α-helix359-37416
α-helix1061-107616
α-helix1077-10826
α-helix1086-110621
α-helix1114-112613
α-helix2036-205419
β-strand2064-2065211
α-helix2066-20672
β-strand2068-2069212
β-strand2074-2075212
β-strand2078-2079211
β-strand2082-2087613
α-helix2088-20892
β-strand2092114
β-strand2100-2105613
β-strand2111113
β-strand2113-2114215
β-strand2119-2120215
β-strand2123113
Chain B: 1 helix, 1 β-strand
ElementResiduesLengthSheet
β-strand39114
α-helix44-474

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Maltose transporter subunit, Receptor activity-modifying protein 2, Calcitonin gene-related…Aprotein591Escherichia coli, Homo sapiensO60895 (AlphaFold model), P0AEX9 (AlphaFold model), Q16602 (AlphaFold model)
AdrenomedullinBprotein29Homo sapiensP35318 (AlphaFold model)
Sequence of entity 1 (A), FASTA
>4RWF_1 Maltose transporter subunit, Receptor activity-modifying protein 2, Calcitonin gene-related peptide type 1 receptor fusion protein (chains A)
MAKIEEGKLVIWINGDKGYNGLAEVGKKFEKDTGIKVTVEHPDKLEEKFPQVAATGDGPD
IIFWAHDRFGGYAQSGLLAEITPDKAFQDKLYPFTWDAVRYNGKLIAYPIAVEALSLIYN
KDLLPNPPKTWEEIPALDKELKAKGKSALMFNLQEPYFTWPLIAADGGYAFKYENGKYDI
KDVGVDNAGAKAGLTFLVDLIKNKHMNADTDYSIAEAAFNKGETAMTINGPWAWSNIDTS
KVNYGVTVLPTFKGQPSKPFVGVLSAGINAASPNKELAKEFLENYLLTDEGLEAVNKDKP
LGAVALKSYEEELAKDPRIAATMENAQKGEIMPNIPQMSAFWYAVRTAVINAASGRQTVD
EALKDAQTNAAAEFGGTVKNYETAVQFCWNHYKDQMDPIEKDWCDWAMISRPYSTLRDCL
EHFAERFDLGFPNPLAERIIFETHQIHFANCSLVQPTFSDGSAGSAGSAEDSIQLGVTRN
KIMTAQYECYQKIMQDPIQQAEGVYCNRTWDGWLCWNDVAAGTESMQLCPDYFQDFDPSE
KVTKICDQDGNWFRHPASNRTWTNYTQCNVNTHEKVKTALNLFYLHHHHHH
Sequence of entity 2 (B), FASTA
>4RWF_2 Adrenomedullin (chains B)
KLAHQIYQFTDKDKDNVAPRSKISPQGYX

Primary citation

Structural Basis for Receptor Activity-Modifying Protein-Dependent Selective Peptide Recognition by a G Protein-Coupled Receptor. Booe, J.M., Walker, C.S., Barwell, J. et al. Mol Cell (2015) 58:1-13. DOI 10.1016/j.molcel.2015.04.018 · PubMed

Other PDB entries of the same protein (UniProt O60895 (AlphaFold model), which also has an AlphaFold model), best resolution first:

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