eF-site ID 3aiy-ABCDEFGHIJKL PDB Code 3aiy Chain A, B, C, D, E, F, G, H, I, J, K, L click to enlarge Title R6 HUMAN INSULIN HEXAMER (SYMMETRIC), NMR, REFINED AVERAGE STRUCTURE Classification HORMONE/GROWTH FACTOR Compound PROTEIN (INSULIN) Source null (INS_HUMAN) Sequence A:  GIVEQCCTSICSLYQLENYCN B:  FVNQHLCGSHLVEALYLVCGERGFFYTPKT C:  GIVEQCCTSICSLYQLENYCN D:  FVNQHLCGSHLVEALYLVCGERGFFYTPKT E:  GIVEQCCTSICSLYQLENYCN F:  FVNQHLCGSHLVEALYLVCGERGFFYTPKT G:  GIVEQCCTSICSLYQLENYCN H:  FVNQHLCGSHLVEALYLVCGERGFFYTPKT I:  GIVEQCCTSICSLYQLENYCN J:  FVNQHLCGSHLVEALYLVCGERGFFYTPKT K:  GIVEQCCTSICSLYQLENYCN L:  FVNQHLCGSHLVEALYLVCGERGFFYTPKT Description Functional site 1) chain B residue 10 type sequence H description IN THE CRYSTAL STRUCTURE, 1ZNJ, THESE RESIDUES ARE COORDINATED BY A ZINC ATOM. THE ZINC ATOM IS NOT INCLUDED SINCE IT COULD NOT BE OBSERVED IN THE NMR SPECTRA. source : ZN1 2) chain F residue 10 type sequence H description IN THE CRYSTAL STRUCTURE, 1ZNJ, THESE RESIDUES ARE COORDINATED BY A ZINC ATOM. THE ZINC ATOM IS NOT INCLUDED SINCE IT COULD NOT BE OBSERVED IN THE NMR SPECTRA. source : ZN1 3) chain J residue 10 type sequence H description IN THE CRYSTAL STRUCTURE, 1ZNJ, THESE RESIDUES ARE COORDINATED BY A ZINC ATOM. THE ZINC ATOM IS NOT INCLUDED SINCE IT COULD NOT BE OBSERVED IN THE NMR SPECTRA. source : ZN1 4) chain D residue 10 type sequence H description IN THE CRYSTAL STRUCTURE, 1ZNJ, THESE RESIDUES ARE COORDINATED BY A ZINC ATOM. THE ZINC ATOM IS NOT INCLUDED SINCE IT COULD NOT BE OBSERVED IN THE NMR SPECTRA. source : ZN2 5) chain H residue 10 type sequence H description IN THE CRYSTAL STRUCTURE, 1ZNJ, THESE RESIDUES ARE COORDINATED BY A ZINC ATOM. THE ZINC ATOM IS NOT INCLUDED SINCE IT COULD NOT BE OBSERVED IN THE NMR SPECTRA. source : ZN2 6) chain L residue 10 type sequence H description IN THE CRYSTAL STRUCTURE, 1ZNJ, THESE RESIDUES ARE COORDINATED BY A ZINC ATOM. THE ZINC ATOM IS NOT INCLUDED SINCE IT COULD NOT BE OBSERVED IN THE NMR SPECTRA. source : ZN2 7) chain A residue 10 type sequence I description BINDING SITE FOR RESIDUE IPH A 22 source : AC1 8) chain A residue 11 type sequence C description BINDING SITE FOR RESIDUE IPH A 22 source : AC1 9) chain A residue 16 type sequence L description BINDING SITE FOR RESIDUE IPH A 22 source : AC1 10) chain B residue 11 type sequence L description BINDING SITE FOR RESIDUE IPH A 22 source : AC1 11) chain B residue 14 type sequence A description BINDING SITE FOR RESIDUE IPH A 22 source : AC1 12) chain F residue 6 type sequence L description BINDING SITE FOR RESIDUE IPH A 22 source : AC1 13) chain H residue 17 type sequence L description BINDING SITE FOR RESIDUE IPH A 22 source : AC1 14) chain C residue 10 type sequence I description BINDING SITE FOR RESIDUE IPH C 22 source : AC2 15) chain C residue 11 type sequence C description BINDING SITE FOR RESIDUE IPH C 22 source : AC2 16) chain C residue 16 type sequence L description BINDING SITE FOR RESIDUE IPH C 22 source : AC2 17) chain D residue 11 type sequence L description BINDING SITE FOR RESIDUE IPH C 22 source : AC2 18) chain D residue 14 type sequence A description BINDING SITE FOR RESIDUE IPH C 22 source : AC2 19) chain J residue 17 type sequence L description BINDING SITE FOR RESIDUE IPH C 22 source : AC2 20) chain L residue 6 type sequence L description BINDING SITE FOR RESIDUE IPH C 22 source : AC2 21) chain E residue 10 type sequence I description BINDING SITE FOR RESIDUE IPH E 22 source : AC3 22) chain E residue 11 type sequence C description BINDING SITE FOR RESIDUE IPH E 22 source : AC3 23) chain E residue 16 type sequence L description BINDING SITE FOR RESIDUE IPH E 22 source : AC3 24) chain F residue 11 type sequence L description BINDING SITE FOR RESIDUE IPH E 22 source : AC3 25) chain F residue 14 type sequence A description BINDING SITE FOR RESIDUE IPH E 22 source : AC3 26) chain J residue 6 type sequence L description BINDING SITE FOR RESIDUE IPH E 22 source : AC3 27) chain L residue 17 type sequence L description BINDING SITE FOR RESIDUE IPH E 22 source : AC3 28) chain B residue 17 type sequence L description BINDING SITE FOR RESIDUE IPH G 22 source : AC4 29) chain D residue 6 type sequence L description BINDING SITE FOR RESIDUE IPH G 22 source : AC4 30) chain G residue 10 type sequence I description BINDING SITE FOR RESIDUE IPH G 22 source : AC4 31) chain G residue 11 type sequence C description BINDING SITE FOR RESIDUE IPH G 22 source : AC4 32) chain G residue 16 type sequence L description BINDING SITE FOR RESIDUE IPH G 22 source : AC4 33) chain H residue 11 type sequence L description BINDING SITE FOR RESIDUE IPH G 22 source : AC4 34) chain H residue 14 type sequence A description BINDING SITE FOR RESIDUE IPH G 22 source : AC4 35) chain B residue 6 type sequence L description BINDING SITE FOR RESIDUE IPH I 22 source : AC5 36) chain D residue 17 type sequence L description BINDING SITE FOR RESIDUE IPH I 22 source : AC5 37) chain I residue 10 type sequence I description BINDING SITE FOR RESIDUE IPH I 22 source : AC5 38) chain I residue 11 type sequence C description BINDING SITE FOR RESIDUE IPH I 22 source : AC5 39) chain I residue 16 type sequence L description BINDING SITE FOR RESIDUE IPH I 22 source : AC5 40) chain J residue 11 type sequence L description BINDING SITE FOR RESIDUE IPH I 22 source : AC5 41) chain J residue 14 type sequence A description BINDING SITE FOR RESIDUE IPH I 22 source : AC5 42) chain F residue 17 type sequence L description BINDING SITE FOR RESIDUE IPH K 22 source : AC6 43) chain H residue 6 type sequence L description BINDING SITE FOR RESIDUE IPH K 22 source : AC6 44) chain K residue 10 type sequence I description BINDING SITE FOR RESIDUE IPH K 22 source : AC6 45) chain K residue 11 type sequence C description BINDING SITE FOR RESIDUE IPH K 22 source : AC6 46) chain K residue 16 type sequence L description BINDING SITE FOR RESIDUE IPH K 22 source : AC6 47) chain L residue 11 type sequence L description BINDING SITE FOR RESIDUE IPH K 22 source : AC6 48) chain L residue 14 type sequence A description BINDING SITE FOR RESIDUE IPH K 22 source : AC6 49) chain A residue 6-20 type prosite sequence CCTSICSLYQLENYC description INSULIN Insulin family signature. CCTSiCSlyqLenyC source prosite : PS00262

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