6V2E: PDB entry 6V2E

Crystal structure of the human CLR:RAMP2 extracellular domain heterodimer with bound high-affinity adrenomedullin S45R/K46L/S48G/Q50W variant. Determined by X-ray diffraction at 1.83 Å resolution. Released 5 Aug 2020.

Method
X-ray diffraction
Resolution
1.83 Å
Organisms
Escherichia coli (strain K12), Homo sapiens
Chains
2
Atoms
5,264
Mol. weight
68.66 kDa
Ligands
NH2
Released
5 Aug 2020

Explore 6V2E in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

6V2E contains 34 α-helices and 36 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: 33 helices, 35 β-strands

ElementResiduesLengthSheet
α-helix4-52
β-strand9-1241
α-helix19-3315
β-strand37-4041
α-helix45-539
β-strand61-6551
α-helix66-683
α-helix69-746
β-strand7812
α-helix85-895
β-strand9113
α-helix93-986
β-strand100-10124
β-strand104-10524
β-strand108-11361
β-strand116-12055
β-strand13016
α-helix131-1333
α-helix134-1429
β-strand147-14935
α-helix156-1583
α-helix160-1656
β-strand169-17467
β-strand177-18487
α-helix188-20215
α-helix212-2209
β-strand224-22965
α-helix231-2333
α-helix234-2407
β-strand244-24745
α-helix248-2503
β-strand25116
β-strand25218
β-strand25518
α-helix2591
β-strand260-26129
β-strand262-26871
β-strand26912
α-helix275-2817
α-helix282-2865
α-helix289-29810
β-strand303-30421
β-strand30613
α-helix307-3137
α-helix317-32812
β-strand330-33129
α-helix332-3332
α-helix338-35316
α-helix359-37416
α-helix1061-107616
α-helix1077-10826
α-helix1086-110621
α-helix1114-112613
α-helix2033-20353
α-helix2036-205015
α-helix2052-20543
β-strand2064-2065210
β-strand2068-2069211
β-strand2074-2075211
β-strand2078-2079210
β-strand2082-2087612
α-helix2088-20892
β-strand2092113
β-strand2100-2105612
β-strand2111112
β-strand2113-2114214
β-strand2119-2120214
β-strand2123112
Chain B: 1 helix, 1 β-strand
ElementResiduesLengthSheet
β-strand39113
α-helix44-474

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Maltose/maltodextrin-binding periplasmic protein,Receptor activity-modifying protein 2,Calcitonin…Aprotein591Escherichia coli (strain K12), Homo sapiensO60895 (AlphaFold model), P0AEX9 (AlphaFold model), Q16602 (AlphaFold model)
ADMBprotein16Homo sapiensP35318 (AlphaFold model)
Sequence of entity 1 (A), FASTA
>6V2E_1 Maltose/maltodextrin-binding periplasmic protein,Receptor activity-modifying protein 2,Calcitonin gene-related peptide type 1 receptor (chains A)
MAKIEEGKLVIWINGDKGYNGLAEVGKKFEKDTGIKVTVEHPDKLEEKFPQVAATGDGPD
IIFWAHDRFGGYAQSGLLAEITPDKAFQDKLYPFTWDAVRYNGKLIAYPIAVEALSLIYN
KDLLPNPPKTWEEIPALDKELKAKGKSALMFNLQEPYFTWPLIAADGGYAFKYENGKYDI
KDVGVDNAGAKAGLTFLVDLIKNKHMNADTDYSIAEAAFNKGETAMTINGPWAWSNIDTS
KVNYGVTVLPTFKGQPSKPFVGVLSAGINAASPNKELAKEFLENYLLTDEGLEAVNKDKP
LGAVALKSYEEELAKDPRIAATMENAQKGEIMPNIPQMSAFWYAVRTAVINAASGRQTVD
EALKDAQTNAAAEFGGTVKNYETAVQFCWNHYKDQMDPIEKDWCDWAMISRPYSTLRDCL
EHFAERFDLGFPNPLAERIIFETHQIHFANCSLVQPTFSDGSAGSAGSAEDSIQLGVTRN
KIMTAQYECYQKIMQDPIQQAEGVYCNRTWDGWLCWNDVAAGTESMQLCPDYFQDFDPSE
KVTKICDQDGNWFRHPASNRTWTNYTQCNVNTHEKVKTALNLFYLHHHHHH
Sequence of entity 2 (B), FASTA
>6V2E_2 ADM (chains B)
DKDNVAPRRLIGPWGY

Ligands and cofactors

IDNameFormulaCopies
NH2Amino groupH2 N1

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

Primary citation

Picomolar Affinity Antagonist and Sustained Signaling Agonist Peptide Ligands for the Adrenomedullin and Calcitonin Gene-Related Peptide Receptors. Booe, J.M., Warner, M.L., Pioszak, A.A. Acs Pharmacol Transl Sci (2020) 3:759-772. DOI 10.1021/acsptsci.0c00031 · 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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