Protein information for: OR2B11



MKSDNHSFLGDSPKAFILLGVSDRPWLELPLFVVLLLSYVLAMLGNVAII
LASRVDPQLHSPMYIFLSHLSFLDLCYTTTTVPQMLVNMGSSQKTISYGG
CTVQYAVFHWLGCTECIVLAAMALDRYVAICKPLHYAVLMHRALCQQLVA
LAWLSGFGNSFVQVVLTVQLPFCGRQVLNNFFCEVPAVIKLSCADTAVND
TILAVLVAFFVLVPLALILLSYGFIARAVLRIQSSKGRHKAFGTCSSHLM
IVSLFYLPAIYMYLQPPSSYSQEQGKFISLFYSIITPTLNPFTYTLRNKD
MKGALRRLLARIWRLCG
In red: predicted N-glycosylation site.
In magenta: Conserved cysteines that are predicted to form a disulfide bond.
Underlined and bold: TM regions.

Predicted binding site residues (CDRs) are highlighted according to the following amino acid color code:
| | basic (H,R,K)
| | hydrophilic, no charge (Q,N,T,S)
| | aliphatic (M,A,I,L,V)
| | aromatic (F,Y,W)
| | helix breakers (G,P)
| | acidic (D,E)
| | cysteine (C)

Sequences of the TM regions:

TM

Start position

End position

Sequence

TM1 28 54 ELPLFVVLLLSYVLAMLGNVAIILASR
TM2 65 87 IFLSHLSFLDLCYTTTTVPQMLV
TM3 102 122 TVQYAVFHWLGCTECIVLAAM
TM4 145 165 CQQLVALAWLSGFGNSFVQVV
TM5 202 223 ILAVLVAFFVLVPLALILLSYG
TM6 245 269 CSSHLMIVSLFYLPAIYMYLQPPSS
TM7 275 294 GKFISLFYSIITPTLNPFTY

The information was derived from a multiple alignment of ORs, based on the algorithms of Man et al. Protein Sci. 2004 Jan;13(1):240-54.
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