eF-site ID 3b3q-ABEF PDB Code 3b3q Chain A, B, E, F click to enlarge Title Crystal structure of a synaptic adhesion complex Classification CELL ADHESION Compound Nlgn1 protein Source (A4FVB9_HUMAN) Sequence A:  DPLVTTNFGKIRGIKKELNNEILGPVIQFLGVPYAAPPTG EHRFQPPEPPSPWSDIRNATQFAPVCPQNIIDGRLPEVML PVWFTNNLDVVSSYVQDQSEDCLYLNIYVPTEDGGPKPVM VYIHGGSYMEGTGNLYDGSVLASYGNVIVITVNYRLGVLG FLSTGDQAAKGNYGLLDLIQALRWTSENIGFFGGDPLRIT VFGSGAGGSCVNLLTLSHYSEGLFQRAIAQSGTALSSWAV SFQPAKYARILATKVGCQVSDTVELVECLQKKPYKELVDQ DVQPARYHIAFGPVIDGDVIPDDPQILMEQGEFLNYDIML GVNQGEGLKFVENIVDSDDGVSASDFDFAVSNFVDNLYGY DVLRETIKFMYTDWADRHNPETRRKTLLALFTDHQWVAPA VATADLHSNFGSPTYFYAFYHHCQTDQVPAWADAAHGDEV PYVLGIPMIGPTELFPCNFSKNDVMLSAVVMTYWTNFAKT GDPNQPVPQDFEEVAWTRYSQKDQLYLHIGLKPRVKEHYR ANKVNLWLELVPHLHN B:  DPLVTTNFGKIRGIKKELNNEILGPVIQFLGVPYAAPPTG EHRFQPPEPPSPWSDIRNATQFAPVCPQNIIDGRLPEVML PVWFTNNLDVVSSYVQDQSEDCLYLNIYVPTEDGGPKPVM VYIHGGSYMEGTGNLYDGSVLASYGNVIVITVNYRLGVLG FLSTGDQAAKGNYGLLDLIQALRWTSENIGFFGGDPLRIT VFGSGAGGSCVNLLTLSHYSEGLFQRAIAQSGTALSSWAV SFQPAKYARILATKVGCQVSDTVELVECLQKKPYKELVDQ DVQPARYHIAFGPVIDGDVIPDDPQILMEQGEFLNYDIML GVNQGEGLKFVENIVDSDDGVSASDFDFAVSNFVDNLYGY DVLRETIKFMYTDWADRHNPETRRKTLLALFTDHQWVAPA VATADLHSNFGSPTYFYAFYHHCQTDQVPAWADAAHGDEV PYVLGIPMIGPTELFPCNFSKNDVMLSAVVMTYWTNFAKT GDPNQPVPQDFEEVAWTRYSQKDQLYLHIGLKPRVKEHYR ANKVNLWLELVPHLHN E:  HSAFAADPGHTTYIFSKGGGQITYKWPPNDRPSTRADRLA IGFSTVQKEAVLVRVDSSSGLGDYLELHIHQGKIGVKFNV GTDDIAIEESNAIINDGKYHVVRFTRSGGNATLQVDSWPV IERYPAGRQLTIFNSQATIIIGGKEQGQPFQGQLSGLYYN GLKVLNMAAENDANIAIVGNVRLVGEV F:  HSAFAADPGHTTYIFSKGGGQITYKWPPNDRPSTRADRLA IGFSTVQKEAVLVRVDSSSGLGDYLELHIHQGKIGVKFNV GTDDIAIEESNAIINDGKYHVVRFTRSGGNATLQVDSWPV IERYPAGRQLTIFNSQATIIIGGKEQGQPFQGQLSGLYYN GLKVLNMAAENDANIAIVGNVRLVGEV Description Functional site 1) chain E residue 184 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000255 source Swiss-Prot : SWS_FT_FI2 2) chain F residue 184 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000255 source Swiss-Prot : SWS_FT_FI2 3) chain B residue 332 type CARBOHYD sequence Y description N-linked (GlcNAc...) asparagine => ECO:0000255 source Swiss-Prot : SWS_FT_FI2 4) chain B residue 372 type CARBOHYD sequence Y description N-linked (GlcNAc...) asparagine => ECO:0000255 source Swiss-Prot : SWS_FT_FI2 5) chain A residue 576 type CARBOHYD sequence V description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:18084303 source Swiss-Prot : SWS_FT_FI3 6) chain B residue 576 type CARBOHYD sequence V description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:18084303 source Swiss-Prot : SWS_FT_FI3 7) chain E residue 137 type BINDING sequence D description BINDING => ECO:0000269|PubMed:18084303 source Swiss-Prot : SWS_FT_FI1 8) chain E residue 154 type BINDING sequence V description BINDING => ECO:0000269|PubMed:18084303 source Swiss-Prot : SWS_FT_FI1 9) chain E residue 266 type BINDING sequence L description BINDING => ECO:0000269|PubMed:18084303 source Swiss-Prot : SWS_FT_FI1 10) chain E residue 268 type BINDING sequence V description BINDING => ECO:0000269|PubMed:18084303 source Swiss-Prot : SWS_FT_FI1 11) chain F residue 137 type BINDING sequence D description BINDING => ECO:0000269|PubMed:18084303 source Swiss-Prot : SWS_FT_FI1 12) chain F residue 154 type BINDING sequence V description BINDING => ECO:0000269|PubMed:18084303 source Swiss-Prot : SWS_FT_FI1 13) chain F residue 266 type BINDING sequence L description BINDING => ECO:0000269|PubMed:18084303 source Swiss-Prot : SWS_FT_FI1 14) chain F residue 268 type BINDING sequence V description BINDING => ECO:0000269|PubMed:18084303 source Swiss-Prot : SWS_FT_FI1 15) chain A residue 151-161 type prosite sequence EDCLYLNIYVP description CARBOXYLESTERASE_B_2 Carboxylesterases type-B signature 2. EDCLYLNIYvP source prosite : PS00941

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