eF-site ID 4aiy-ABCDEFGHIJKL PDB Code 4aiy Chain A, B, C, D, E, F, G, H, I, J, K, L click to enlarge Title R6 HUMAN INSULIN HEXAMER (SYMMETRIC), NMR, 'GREEN' SUBSTATE, 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 6 type sequence C description BINDING SITE FOR RESIDUE IPH A 22 source : AC1 8) chain A residue 10 type sequence I description BINDING SITE FOR RESIDUE IPH A 22 source : AC1 9) chain A residue 11 type sequence C 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 H residue 17 type sequence L description BINDING SITE FOR RESIDUE IPH A 22 source : AC1 13) chain C residue 6 type sequence C description BINDING SITE FOR RESIDUE IPH C 22 source : AC2 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 D residue 11 type sequence L description BINDING SITE FOR RESIDUE IPH C 22 source : AC2 17) chain D residue 14 type sequence A description BINDING SITE FOR RESIDUE IPH C 22 source : AC2 18) chain J residue 17 type sequence L description BINDING SITE FOR RESIDUE IPH C 22 source : AC2 19) chain E residue 6 type sequence C description BINDING SITE FOR RESIDUE IPH E 22 source : AC3 20) chain E residue 10 type sequence I description BINDING SITE FOR RESIDUE IPH E 22 source : AC3 21) chain E residue 11 type sequence C description BINDING SITE FOR RESIDUE IPH E 22 source : AC3 22) chain F residue 11 type sequence L description BINDING SITE FOR RESIDUE IPH E 22 source : AC3 23) chain F residue 14 type sequence A description BINDING SITE FOR RESIDUE IPH E 22 source : AC3 24) chain L residue 17 type sequence L description BINDING SITE FOR RESIDUE IPH E 22 source : AC3 25) chain B residue 17 type sequence L description BINDING SITE FOR RESIDUE IPH G 22 source : AC4 26) chain G residue 6 type sequence C description BINDING SITE FOR RESIDUE IPH G 22 source : AC4 27) chain G residue 10 type sequence I description BINDING SITE FOR RESIDUE IPH G 22 source : AC4 28) chain G residue 11 type sequence C description BINDING SITE FOR RESIDUE IPH G 22 source : AC4 29) chain H residue 11 type sequence L description BINDING SITE FOR RESIDUE IPH G 22 source : AC4 30) chain H residue 14 type sequence A description BINDING SITE FOR RESIDUE IPH G 22 source : AC4 31) chain D residue 17 type sequence L description BINDING SITE FOR RESIDUE IPH I 22 source : AC5 32) chain I residue 6 type sequence C description BINDING SITE FOR RESIDUE IPH I 22 source : AC5 33) chain I residue 10 type sequence I description BINDING SITE FOR RESIDUE IPH I 22 source : AC5 34) chain I residue 11 type sequence C description BINDING SITE FOR RESIDUE IPH I 22 source : AC5 35) chain J residue 11 type sequence L description BINDING SITE FOR RESIDUE IPH I 22 source : AC5 36) chain J residue 14 type sequence A description BINDING SITE FOR RESIDUE IPH I 22 source : AC5 37) chain F residue 17 type sequence L description BINDING SITE FOR RESIDUE IPH K 22 source : AC6 38) chain K residue 6 type sequence C description BINDING SITE FOR RESIDUE IPH K 22 source : AC6 39) chain K residue 10 type sequence I description BINDING SITE FOR RESIDUE IPH K 22 source : AC6 40) chain K residue 11 type sequence C description BINDING SITE FOR RESIDUE IPH K 22 source : AC6 41) chain L residue 11 type sequence L description BINDING SITE FOR RESIDUE IPH K 22 source : AC6 42) chain L residue 14 type sequence A description BINDING SITE FOR RESIDUE IPH K 22 source : AC6 43) chain A residue 6-20 type prosite sequence CCTSICSLYQLENYC description INSULIN Insulin family signature. CCTSiCSlyqLenyC source prosite : PS00262

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