eF-site ID 6dld-ABCD PDB Code 6dld Chain A, B, C, D click to enlarge Title Crystal structure of IgLON5/NEGR1 heterodimer Classification CELL ADHESION Compound IgLON family member 5 Source (NEGR1_HUMAN) Sequence A:  NSPADNYTVCEGDNATLSCFIDEHVTRVAWLNRSNILYAG NDRWTSDPRVRLLINTPEEFSILITEVGLGDEGLYTCSFQ TRHQPYTTQVYLIVHVPARIVNISSPVTVNEGGNVNLLCL AVGRPEPTVTWRQLRDGFTSEGEILEISDIQRGQAGEYEC VTHNGVNSAPDSRRVLVTVNYPPTITDVTSARTALGRAAL LRCEAMAVPPADFQWYKDDRLLSSGTAEGLKVQTERTRSM LLFANVSARHYGNYTCRAANRLGASSASMRLLR B:  AAVDNMMVRKGDTAVLRCYLEDGASKGAWLNRSSIIFAGG DKWSVDPRVSISTLNKRDYSLQIQNVDVTDDGPYTCSVQT QHTPRTMQVHLTVQVPPKIYDISNDMTVNEGTNVTLTCLA TGKPEPSISWRHISPSAKPFENGQYLDIYGITRDQAGEYE CSAENDVSFPDVRKVKVVVNFAPTIQEICEGAGVPPPAFE WYKGEKKLFNFSTRSILTVTNVTQEHFGNYTCVAANKLGT TNASLPL C:  PADNYTVCEGDNATLSCFIDEHVTRVAWLNRSNILYAGND RWTSDPRVRLLINTPEEFSILITEVGLGDEGLYTCSFQTR HQPYTTQVYLIVHVPARIVNISSPVTVNEGGNVNLLCLAV GRPEPTVTWRQLRDGFTSEGEILEISDIQRGQAGEYECVT HNGVNSAPDSRRVLVTVNYPPTITDVTSARTALGRAALLR CEAMAVPPADFQWYKDDRLLSSGTAEGLKVQTERTRSMLL FANVSARHYGNYTCRAANRLGASSASM D:  AVDFPWAAVDNMMVRKGDTAVLRCYLEDGASKGAWLNRSS IIFAGGDKWSVDPRVSISTLNKRDYSLQIQNVDVTDDGPY TCSVQTQHTPRTMQVHLTVQVPPKIYDISNDMTVNEGTNV TLTCLATGKPEPSISWRHISPSAKPFENGQYLDIYGITRD QAGEYECSAENDVSFPDVRKVKVVVNFAPTIQEIKSGTLI RCEGAGVPPPAFEWYKGEKKLFNGQQGIIIQNFSTRSILT VTNVTQEHFGNYTCVAANKLGTTNASLPL Description Functional site 1) chain B residue 73 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000255 source Swiss-Prot : SWS_FT_FI3 2) chain D residue 286 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000255 source Swiss-Prot : SWS_FT_FI3 3) chain D residue 294 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000255 source Swiss-Prot : SWS_FT_FI3 4) chain D residue 307 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000255 source Swiss-Prot : SWS_FT_FI3 5) chain B residue 155 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000255 source Swiss-Prot : SWS_FT_FI3 6) chain B residue 275 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000255 source Swiss-Prot : SWS_FT_FI3 7) chain B residue 286 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000255 source Swiss-Prot : SWS_FT_FI3 8) chain B residue 294 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000255 source Swiss-Prot : SWS_FT_FI3 9) chain B residue 307 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000255 source Swiss-Prot : SWS_FT_FI3 10) chain D residue 73 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000255 source Swiss-Prot : SWS_FT_FI3 11) chain D residue 155 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000255 source Swiss-Prot : SWS_FT_FI3 12) chain D residue 275 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000255 source Swiss-Prot : SWS_FT_FI3 13) chain B residue 187 type MOD_RES sequence Y description Phosphotyrosine => ECO:0000250|UniProtKB:Q80Z24 source Swiss-Prot : SWS_FT_FI1 14) chain C residue 288 type MOD_RES sequence N description Phosphotyrosine => ECO:0000250|UniProtKB:Q80Z24 source Swiss-Prot : SWS_FT_FI1 15) chain D residue 187 type MOD_RES sequence Y description Phosphotyrosine => ECO:0000250|UniProtKB:Q80Z24 source Swiss-Prot : SWS_FT_FI1 16) chain A residue 67 type MOD_RES sequence N description Phosphotyrosine => ECO:0000250|UniProtKB:Q80Z24 source Swiss-Prot : SWS_FT_FI1 17) chain A residue 137 type MOD_RES sequence N description Phosphotyrosine => ECO:0000250|UniProtKB:Q80Z24 source Swiss-Prot : SWS_FT_FI1 18) chain A residue 288 type MOD_RES sequence N description Phosphotyrosine => ECO:0000250|UniProtKB:Q80Z24 source Swiss-Prot : SWS_FT_FI1 19) chain C residue 41 type MOD_RES sequence N description Phosphotyrosine => ECO:0000250|UniProtKB:Q80Z24 source Swiss-Prot : SWS_FT_FI1 20) chain C residue 49 type MOD_RES sequence N description Phosphotyrosine => ECO:0000250|UniProtKB:Q80Z24 source Swiss-Prot : SWS_FT_FI1 21) chain C residue 67 type MOD_RES sequence N description Phosphotyrosine => ECO:0000250|UniProtKB:Q80Z24 source Swiss-Prot : SWS_FT_FI1 22) chain C residue 137 type MOD_RES sequence N description Phosphotyrosine => ECO:0000250|UniProtKB:Q80Z24 source Swiss-Prot : SWS_FT_FI1

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