eF-site ID 6cu7-ABCDEFGHIJ PDB Code 6cu7 Chain A, B, C, D, E, F, G, H, I, J click to enlarge Title Alpha Synuclein fibril formed by full length protein - Rod Polymorph Classification PROTEIN FIBRIL Compound Alpha-synuclein Source (SYUA_HUMAN) Sequence A:  LYVGSKTKEGVVHGVATVAEKTKEQVTNVGGAVVTGVTAV AQKTVEGAGSIAAATGFVKK B:  LYVGSKTKEGVVHGVATVAEKTKEQVTNVGGAVVTGVTAV AQKTVEGAGSIAAATGFVKK C:  LYVGSKTKEGVVHGVATVAEKTKEQVTNVGGAVVTGVTAV AQKTVEGAGSIAAATGFVKK D:  LYVGSKTKEGVVHGVATVAEKTKEQVTNVGGAVVTGVTAV AQKTVEGAGSIAAATGFVKK E:  LYVGSKTKEGVVHGVATVAEKTKEQVTNVGGAVVTGVTAV AQKTVEGAGSIAAATGFVKK F:  LYVGSKTKEGVVHGVATVAEKTKEQVTNVGGAVVTGVTAV AQKTVEGAGSIAAATGFVKK G:  LYVGSKTKEGVVHGVATVAEKTKEQVTNVGGAVVTGVTAV AQKTVEGAGSIAAATGFVKK H:  LYVGSKTKEGVVHGVATVAEKTKEQVTNVGGAVVTGVTAV AQKTVEGAGSIAAATGFVKK I:  LYVGSKTKEGVVHGVATVAEKTKEQVTNVGGAVVTGVTAV AQKTVEGAGSIAAATGFVKK J:  LYVGSKTKEGVVHGVATVAEKTKEQVTNVGGAVVTGVTAV AQKTVEGAGSIAAATGFVKK Description Functional site 1) chain D residue 50 type BINDING sequence H description BINDING => ECO:0000305 source Swiss-Prot : SWS_FT_FI1 2) chain F residue 50 type BINDING sequence H description BINDING => ECO:0000305 source Swiss-Prot : SWS_FT_FI1 3) chain G residue 50 type BINDING sequence H description BINDING => ECO:0000305 source Swiss-Prot : SWS_FT_FI1 4) chain H residue 50 type BINDING sequence H description BINDING => ECO:0000305 source Swiss-Prot : SWS_FT_FI1 5) chain I residue 50 type BINDING sequence H description BINDING => ECO:0000305 source Swiss-Prot : SWS_FT_FI1 6) chain E residue 50 type BINDING sequence H description BINDING => ECO:0000305 source Swiss-Prot : SWS_FT_FI1 7) chain J residue 50 type BINDING sequence H description BINDING => ECO:0000305 source Swiss-Prot : SWS_FT_FI1 8) chain A residue 50 type BINDING sequence H description BINDING => ECO:0000305 source Swiss-Prot : SWS_FT_FI1 9) chain B residue 50 type BINDING sequence H description BINDING => ECO:0000305 source Swiss-Prot : SWS_FT_FI1 10) chain C residue 50 type BINDING sequence H description BINDING => ECO:0000305 source Swiss-Prot : SWS_FT_FI1 11) chain E residue 87 type MOD_RES sequence S description Phosphoserine => ECO:0000269|PubMed:10617630 source Swiss-Prot : SWS_FT_FI3 12) chain J residue 87 type MOD_RES sequence S description Phosphoserine => ECO:0000269|PubMed:10617630 source Swiss-Prot : SWS_FT_FI3 13) chain A residue 87 type MOD_RES sequence S description Phosphoserine => ECO:0000269|PubMed:10617630 source Swiss-Prot : SWS_FT_FI3 14) chain B residue 87 type MOD_RES sequence S description Phosphoserine => ECO:0000269|PubMed:10617630 source Swiss-Prot : SWS_FT_FI3 15) chain C residue 87 type MOD_RES sequence S description Phosphoserine => ECO:0000269|PubMed:10617630 source Swiss-Prot : SWS_FT_FI3 16) chain D residue 87 type MOD_RES sequence S description Phosphoserine => ECO:0000269|PubMed:10617630 source Swiss-Prot : SWS_FT_FI3 17) chain F residue 87 type MOD_RES sequence S description Phosphoserine => ECO:0000269|PubMed:10617630 source Swiss-Prot : SWS_FT_FI3 18) chain G residue 87 type MOD_RES sequence S description Phosphoserine => ECO:0000269|PubMed:10617630 source Swiss-Prot : SWS_FT_FI3 19) chain H residue 87 type MOD_RES sequence S description Phosphoserine => ECO:0000269|PubMed:10617630 source Swiss-Prot : SWS_FT_FI3 20) chain I residue 87 type MOD_RES sequence S description Phosphoserine => ECO:0000269|PubMed:10617630 source Swiss-Prot : SWS_FT_FI3

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