eF-site ID 1ji4-ABCDEFGHIJKL PDB Code 1ji4 Chain A, B, C, D, E, F, G, H, I, J, K, L click to enlarge Title NAP protein from helicobacter pylori Classification METAL TRANSPORT Compound NEUTROPHIL-ACTIVATING PROTEIN A Source Helicobacter pylori (Campylobacter pylori) (NAPA_HELPY) Sequence A:  MKTFEILKHLQADAIVLFMKVHNFHWNVKGTDFFNVHKAT EEIYEEFADMFDDLAERIVQLGHHPLVTLSEAIKLTRVKE ETKTSFHSKDIFKEILEDYKYLEKEFKELSNTAEKEGDKV TVTYADDQLAKLQKSIWMLQAHLA B:  MKTFEILKHLQADAIVLFMKVHNFHWNVKGTDFFNVHKAT EEIYEEFADMFDDLAERIVQLGHHPLVTLSEAIKLTRVKE ETKTSFHSKDIFKEILEDYKYLEKEFKELSNTAEKEGDKV TVTYADDQLAKLQKSIWMLQAHLA C:  MKTFEILKHLQADAIVLFMKVHNFHWNVKGTDFFNVHKAT EEIYEEFADMFDDLAERIVQLGHHPLVTLSEAIKLTRVKE ETKTSFHSKDIFKEILEDYKYLEKEFKELSNTAEKEGDKV TVTYADDQLAKLQKSIWMLQAHLA D:  MKTFEILKHLQADAIVLFMKVHNFHWNVKGTDFFNVHKAT EEIYEEFADMFDDLAERIVQLGHHPLVTLSEAIKLTRVKE ETKTSFHSKDIFKEILEDYKYLEKEFKELSNTAEKEGDKV TVTYADDQLAKLQKSIWMLQAHLA E:  MKTFEILKHLQADAIVLFMKVHNFHWNVKGTDFFNVHKAT EEIYEEFADMFDDLAERIVQLGHHPLVTLSEAIKLTRVKE ETKTSFHSKDIFKEILEDYKYLEKEFKELSNTAEKEGDKV TVTYADDQLAKLQKSIWMLQAHLA F:  MKTFEILKHLQADAIVLFMKVHNFHWNVKGTDFFNVHKAT EEIYEEFADMFDDLAERIVQLGHHPLVTLSEAIKLTRVKE ETKTSFHSKDIFKEILEDYKYLEKEFKELSNTAEKEGDKV TVTYADDQLAKLQKSIWMLQAHLA G:  MKTFEILKHLQADAIVLFMKVHNFHWNVKGTDFFNVHKAT EEIYEEFADMFDDLAERIVQLGHHPLVTLSEAIKLTRVKE ETKTSFHSKDIFKEILEDYKYLEKEFKELSNTAEKEGDKV TVTYADDQLAKLQKSIWMLQAHLA H:  MKTFEILKHLQADAIVLFMKVHNFHWNVKGTDFFNVHKAT EEIYEEFADMFDDLAERIVQLGHHPLVTLSEAIKLTRVKE ETKTSFHSKDIFKEILEDYKYLEKEFKELSNTAEKEGDKV TVTYADDQLAKLQKSIWMLQAHLA I:  MKTFEILKHLQADAIVLFMKVHNFHWNVKGTDFFNVHKAT EEIYEEFADMFDDLAERIVQLGHHPLVTLSEAIKLTRVKE ETKTSFHSKDIFKEILEDYKYLEKEFKELSNTAEKEGDKV TVTYADDQLAKLQKSIWMLQAHLA J:  MKTFEILKHLQADAIVLFMKVHNFHWNVKGTDFFNVHKAT EEIYEEFADMFDDLAERIVQLGHHPLVTLSEAIKLTRVKE ETKTSFHSKDIFKEILEDYKYLEKEFKELSNTAEKEGDKV TVTYADDQLAKLQKSIWMLQAHLA K:  MKTFEILKHLQADAIVLFMKVHNFHWNVKGTDFFNVHKAT EEIYEEFADMFDDLAERIVQLGHHPLVTLSEAIKLTRVKE ETKTSFHSKDIFKEILEDYKYLEKEFKELSNTAEKEGDKV TVTYADDQLAKLQKSIWMLQAHLA L:  MKTFEILKHLQADAIVLFMKVHNFHWNVKGTDFFNVHKAT EEIYEEFADMFDDLAERIVQLGHHPLVTLSEAIKLTRVKE ETKTSFHSKDIFKEILEDYKYLEKEFKELSNTAEKEGDKV TVTYADDQLAKLQKSIWMLQAHLA Description Functional site 1) chain A residue 25 type sequence H description BINDING SITE FOR RESIDUE FE D 801 source : AC1 2) chain D residue 52 type sequence D description BINDING SITE FOR RESIDUE FE D 801 source : AC1 3) chain D residue 56 type sequence E description BINDING SITE FOR RESIDUE FE D 801 source : AC1 4) chain B residue 25 type sequence H description BINDING SITE FOR RESIDUE FE C 803 source : AC2 5) chain C residue 52 type sequence D description BINDING SITE FOR RESIDUE FE C 803 source : AC2 6) chain C residue 56 type sequence E description BINDING SITE FOR RESIDUE FE C 803 source : AC2 7) chain B residue 52 type sequence D description BINDING SITE FOR RESIDUE FE B 805 source : AC3 8) chain B residue 56 type sequence E description BINDING SITE FOR RESIDUE FE B 805 source : AC3 9) chain C residue 25 type sequence H description BINDING SITE FOR RESIDUE FE B 805 source : AC3 10) chain A residue 52 type sequence D description BINDING SITE FOR RESIDUE FE A 807 source : AC4 11) chain A residue 56 type sequence E description BINDING SITE FOR RESIDUE FE A 807 source : AC4 12) chain D residue 25 type sequence H description BINDING SITE FOR RESIDUE FE A 807 source : AC4 13) chain E residue 25 type sequence H description BINDING SITE FOR RESIDUE FE H 809 source : AC5 14) chain H residue 52 type sequence D description BINDING SITE FOR RESIDUE FE H 809 source : AC5 15) chain H residue 56 type sequence E description BINDING SITE FOR RESIDUE FE H 809 source : AC5 16) chain F residue 25 type sequence H description BINDING SITE FOR RESIDUE FE G 811 source : AC6 17) chain G residue 52 type sequence D description BINDING SITE FOR RESIDUE FE G 811 source : AC6 18) chain G residue 56 type sequence E description BINDING SITE FOR RESIDUE FE G 811 source : AC6 19) chain F residue 52 type sequence D description BINDING SITE FOR RESIDUE FE F 813 source : AC7 20) chain F residue 56 type sequence E description BINDING SITE FOR RESIDUE FE F 813 source : AC7 21) chain G residue 25 type sequence H description BINDING SITE FOR RESIDUE FE F 813 source : AC7 22) chain E residue 52 type sequence D description BINDING SITE FOR RESIDUE FE E 815 source : AC8 23) chain E residue 56 type sequence E description BINDING SITE FOR RESIDUE FE E 815 source : AC8 24) chain H residue 25 type sequence H description BINDING SITE FOR RESIDUE FE E 815 source : AC8 25) chain I residue 25 type sequence H description BINDING SITE FOR RESIDUE FE L 817 source : AC9 26) chain L residue 52 type sequence D description BINDING SITE FOR RESIDUE FE L 817 source : AC9 27) chain L residue 56 type sequence E description BINDING SITE FOR RESIDUE FE L 817 source : AC9 28) chain J residue 25 type sequence H description BINDING SITE FOR RESIDUE FE K 819 source : BC1 29) chain K residue 52 type sequence D description BINDING SITE FOR RESIDUE FE K 819 source : BC1 30) chain K residue 56 type sequence E description BINDING SITE FOR RESIDUE FE K 819 source : BC1 31) chain J residue 52 type sequence D description BINDING SITE FOR RESIDUE FE J 821 source : BC2 32) chain J residue 56 type sequence E description BINDING SITE FOR RESIDUE FE J 821 source : BC2 33) chain K residue 25 type sequence H description BINDING SITE FOR RESIDUE FE J 821 source : BC2 34) chain I residue 52 type sequence D description BINDING SITE FOR RESIDUE FE I 823 source : BC3 35) chain I residue 56 type sequence E description BINDING SITE FOR RESIDUE FE I 823 source : BC3 36) chain L residue 25 type sequence H description BINDING SITE FOR RESIDUE FE I 823 source : BC3 37) chain A residue 37 type sequence H description BINDING SITE FOR RESIDUE UNX A 802 source : BC4 38) chain G residue 134 type sequence K description BINDING SITE FOR RESIDUE UNX A 802 source : BC4 39) chain B residue 37 type sequence H description BINDING SITE FOR RESIDUE UNX B 804 source : BC5 40) chain E residue 134 type sequence K description BINDING SITE FOR RESIDUE UNX B 804 source : BC5 41) chain C residue 37 type sequence H description BINDING SITE FOR RESIDUE UNX C 806 source : BC6 42) chain F residue 134 type sequence K description BINDING SITE FOR RESIDUE UNX C 806 source : BC6 43) chain D residue 37 type sequence H description BINDING SITE FOR RESIDUE UNX D 808 source : BC7 44) chain H residue 134 type sequence K description BINDING SITE FOR RESIDUE UNX D 808 source : BC7 45) chain E residue 37 type sequence H description BINDING SITE FOR RESIDUE UNX E 810 source : BC8 46) chain K residue 134 type sequence K description BINDING SITE FOR RESIDUE UNX E 810 source : BC8 47) chain F residue 37 type sequence H description BINDING SITE FOR RESIDUE UNX F 812 source : BC9 48) chain I residue 134 type sequence K description BINDING SITE FOR RESIDUE UNX F 812 source : BC9 49) chain G residue 37 type sequence H description BINDING SITE FOR RESIDUE UNX G 814 source : CC1 50) chain J residue 134 type sequence K description BINDING SITE FOR RESIDUE UNX G 814 source : CC1 51) chain H residue 37 type sequence H description BINDING SITE FOR RESIDUE UNX H 816 source : CC2 52) chain L residue 134 type sequence K description BINDING SITE FOR RESIDUE UNX H 816 source : CC2 53) chain C residue 134 type sequence K description BINDING SITE FOR RESIDUE UNX I 818 source : CC3 54) chain I residue 37 type sequence H description BINDING SITE FOR RESIDUE UNX I 818 source : CC3 55) chain L residue 56 type sequence E description BINDING SITE FOR RESIDUE UNX I 818 source : CC3 56) chain J residue 37 type sequence H description BINDING SITE FOR RESIDUE UNX J 820 source : CC4 57) chain K residue 37 type sequence H description BINDING SITE FOR RESIDUE UNX K 822 source : CC5 58) chain D residue 134 type sequence K description BINDING SITE FOR RESIDUE UNX L 824 source : CC6 59) chain I residue 56 type sequence E description BINDING SITE FOR RESIDUE UNX L 824 source : CC6 60) chain L residue 37 type sequence H description BINDING SITE FOR RESIDUE UNX L 824 source : CC6 61) chain A residue 46 type sequence E description BINDING SITE FOR RESIDUE MPD A 700 source : CC7 62) chain A residue 99 type sequence Y description BINDING SITE FOR RESIDUE MPD A 700 source : CC7 63) chain A residue 132 type sequence L description BINDING SITE FOR RESIDUE MPD A 700 source : CC7 64) chain A residue 135 type sequence S description BINDING SITE FOR RESIDUE MPD A 700 source : CC7 65) chain B residue 46 type sequence E description BINDING SITE FOR RESIDUE MPD B 701 source : CC8 66) chain B residue 99 type sequence Y description BINDING SITE FOR RESIDUE MPD B 701 source : CC8 67) chain B residue 132 type sequence L description BINDING SITE FOR RESIDUE MPD B 701 source : CC8 68) chain B residue 135 type sequence S description BINDING SITE FOR RESIDUE MPD B 701 source : CC8 69) chain C residue 46 type sequence E description BINDING SITE FOR RESIDUE MPD C 702 source : CC9 70) chain C residue 99 type sequence Y description BINDING SITE FOR RESIDUE MPD C 702 source : CC9 71) chain C residue 132 type sequence L description BINDING SITE FOR RESIDUE MPD C 702 source : CC9 72) chain C residue 135 type sequence S description BINDING SITE FOR RESIDUE MPD C 702 source : CC9 73) chain D residue 46 type sequence E description BINDING SITE FOR RESIDUE MPD D 703 source : DC1 74) chain D residue 99 type sequence Y description BINDING SITE FOR RESIDUE MPD D 703 source : DC1 75) chain D residue 132 type sequence L description BINDING SITE FOR RESIDUE MPD D 703 source : DC1 76) chain D residue 135 type sequence S description BINDING SITE FOR RESIDUE MPD D 703 source : DC1 77) chain E residue 46 type sequence E description BINDING SITE FOR RESIDUE MPD E 704 source : DC2 78) chain E residue 99 type sequence Y description BINDING SITE FOR RESIDUE MPD E 704 source : DC2 79) chain E residue 132 type sequence L description BINDING SITE FOR RESIDUE MPD E 704 source : DC2 80) chain E residue 135 type sequence S description BINDING SITE FOR RESIDUE MPD E 704 source : DC2 81) chain F residue 46 type sequence E description BINDING SITE FOR RESIDUE MPD F 705 source : DC3 82) chain F residue 99 type sequence Y description BINDING SITE FOR RESIDUE MPD F 705 source : DC3 83) chain F residue 132 type sequence L description BINDING SITE FOR RESIDUE MPD F 705 source : DC3 84) chain F residue 135 type sequence S description BINDING SITE FOR RESIDUE MPD F 705 source : DC3 85) chain G residue 46 type sequence E description BINDING SITE FOR RESIDUE MPD G 706 source : DC4 86) chain G residue 99 type sequence Y description BINDING SITE FOR RESIDUE MPD G 706 source : DC4 87) chain G residue 132 type sequence L description BINDING SITE FOR RESIDUE MPD G 706 source : DC4 88) chain G residue 135 type sequence S description BINDING SITE FOR RESIDUE MPD G 706 source : DC4 89) chain H residue 46 type sequence E description BINDING SITE FOR RESIDUE MPD H 707 source : DC5 90) chain H residue 99 type sequence Y description BINDING SITE FOR RESIDUE MPD H 707 source : DC5 91) chain H residue 132 type sequence L description BINDING SITE FOR RESIDUE MPD H 707 source : DC5 92) chain H residue 135 type sequence S description BINDING SITE FOR RESIDUE MPD H 707 source : DC5 93) chain I residue 46 type sequence E description BINDING SITE FOR RESIDUE MPD I 708 source : DC6 94) chain I residue 99 type sequence Y description BINDING SITE FOR RESIDUE MPD I 708 source : DC6 95) chain I residue 132 type sequence L description BINDING SITE FOR RESIDUE MPD I 708 source : DC6 96) chain I residue 135 type sequence S description BINDING SITE FOR RESIDUE MPD I 708 source : DC6 97) chain J residue 46 type sequence E description BINDING SITE FOR RESIDUE MPD J 709 source : DC7 98) chain J residue 99 type sequence Y description BINDING SITE FOR RESIDUE MPD J 709 source : DC7 99) chain J residue 132 type sequence L description BINDING SITE FOR RESIDUE MPD J 709 source : DC7 100) chain J residue 135 type sequence S description BINDING SITE FOR RESIDUE MPD J 709 source : DC7 101) chain K residue 46 type sequence E description BINDING SITE FOR RESIDUE MPD K 710 source : DC8 102) chain K residue 99 type sequence Y description BINDING SITE FOR RESIDUE MPD K 710 source : DC8 103) chain K residue 132 type sequence L description BINDING SITE FOR RESIDUE MPD K 710 source : DC8 104) chain K residue 135 type sequence S description BINDING SITE FOR RESIDUE MPD K 710 source : DC8 105) chain L residue 46 type sequence E description BINDING SITE FOR RESIDUE MPD L 711 source : DC9 106) chain L residue 99 type sequence Y description BINDING SITE FOR RESIDUE MPD L 711 source : DC9 107) chain L residue 132 type sequence L description BINDING SITE FOR RESIDUE MPD L 711 source : DC9 108) chain L residue 135 type sequence S description BINDING SITE FOR RESIDUE MPD L 711 source : DC9 109) chain A residue 25 type BINDING sequence H description BINDING => ECO:0000269|PubMed:12368104 source Swiss-Prot : SWS_FT_FI1 110) chain J residue 25 type BINDING sequence H description BINDING => ECO:0000269|PubMed:12368104 source Swiss-Prot : SWS_FT_FI1 111) chain K residue 25 type BINDING sequence H description BINDING => ECO:0000269|PubMed:12368104 source Swiss-Prot : SWS_FT_FI1 112) chain L residue 25 type BINDING sequence H description BINDING => ECO:0000269|PubMed:12368104 source Swiss-Prot : SWS_FT_FI1 113) chain B residue 25 type BINDING sequence H description BINDING => ECO:0000269|PubMed:12368104 source Swiss-Prot : SWS_FT_FI1 114) chain C residue 25 type BINDING sequence H description BINDING => ECO:0000269|PubMed:12368104 source Swiss-Prot : SWS_FT_FI1 115) chain D residue 25 type BINDING sequence H description BINDING => ECO:0000269|PubMed:12368104 source Swiss-Prot : SWS_FT_FI1 116) chain E residue 25 type BINDING sequence H description BINDING => ECO:0000269|PubMed:12368104 source Swiss-Prot : SWS_FT_FI1 117) chain F residue 25 type BINDING sequence H description BINDING => ECO:0000269|PubMed:12368104 source Swiss-Prot : SWS_FT_FI1 118) chain G residue 25 type BINDING sequence H description BINDING => ECO:0000269|PubMed:12368104 source Swiss-Prot : SWS_FT_FI1 119) chain H residue 25 type BINDING sequence H description BINDING => ECO:0000269|PubMed:12368104 source Swiss-Prot : SWS_FT_FI1 120) chain I residue 25 type BINDING sequence H description BINDING => ECO:0000269|PubMed:12368104 source Swiss-Prot : SWS_FT_FI1 121) chain A residue 52 type BINDING sequence D description in other chain => ECO:0000269|PubMed:12368104 source Swiss-Prot : SWS_FT_FI2 122) chain J residue 52 type BINDING sequence D description in other chain => ECO:0000269|PubMed:12368104 source Swiss-Prot : SWS_FT_FI2 123) chain K residue 52 type BINDING sequence D description in other chain => ECO:0000269|PubMed:12368104 source Swiss-Prot : SWS_FT_FI2 124) chain L residue 52 type BINDING sequence D description in other chain => ECO:0000269|PubMed:12368104 source Swiss-Prot : SWS_FT_FI2 125) chain B residue 52 type BINDING sequence D description in other chain => ECO:0000269|PubMed:12368104 source Swiss-Prot : SWS_FT_FI2 126) chain C residue 52 type BINDING sequence D description in other chain => ECO:0000269|PubMed:12368104 source Swiss-Prot : SWS_FT_FI2 127) chain D residue 52 type BINDING sequence D description in other chain => ECO:0000269|PubMed:12368104 source Swiss-Prot : SWS_FT_FI2 128) chain E residue 52 type BINDING sequence D description in other chain => ECO:0000269|PubMed:12368104 source Swiss-Prot : SWS_FT_FI2 129) chain F residue 52 type BINDING sequence D description in other chain => ECO:0000269|PubMed:12368104 source Swiss-Prot : SWS_FT_FI2 130) chain G residue 52 type BINDING sequence D description in other chain => ECO:0000269|PubMed:12368104 source Swiss-Prot : SWS_FT_FI2 131) chain H residue 52 type BINDING sequence D description in other chain => ECO:0000269|PubMed:12368104 source Swiss-Prot : SWS_FT_FI2 132) chain I residue 52 type BINDING sequence D description in other chain => ECO:0000269|PubMed:12368104 source Swiss-Prot : SWS_FT_FI2 133) chain A residue 56 type BINDING sequence E description BINDING => ECO:0000255 source Swiss-Prot : SWS_FT_FI3 134) chain J residue 56 type BINDING sequence E description BINDING => ECO:0000255 source Swiss-Prot : SWS_FT_FI3 135) chain K residue 56 type BINDING sequence E description BINDING => ECO:0000255 source Swiss-Prot : SWS_FT_FI3 136) chain L residue 56 type BINDING sequence E description BINDING => ECO:0000255 source Swiss-Prot : SWS_FT_FI3 137) chain B residue 56 type BINDING sequence E description BINDING => ECO:0000255 source Swiss-Prot : SWS_FT_FI3 138) chain C residue 56 type BINDING sequence E description BINDING => ECO:0000255 source Swiss-Prot : SWS_FT_FI3 139) chain D residue 56 type BINDING sequence E description BINDING => ECO:0000255 source Swiss-Prot : SWS_FT_FI3 140) chain E residue 56 type BINDING sequence E description BINDING => ECO:0000255 source Swiss-Prot : SWS_FT_FI3 141) chain F residue 56 type BINDING sequence E description BINDING => ECO:0000255 source Swiss-Prot : SWS_FT_FI3 142) chain G residue 56 type BINDING sequence E description BINDING => ECO:0000255 source Swiss-Prot : SWS_FT_FI3 143) chain H residue 56 type BINDING sequence E description BINDING => ECO:0000255 source Swiss-Prot : SWS_FT_FI3 144) chain I residue 56 type BINDING sequence E description BINDING => ECO:0000255 source Swiss-Prot : SWS_FT_FI3 145) chain A residue 25-41 type prosite sequence HWNVKGTDFFNVHKATE description DPS_1 Dps protein family signature 1. HWnVkGtdffnVHkatE source prosite : PS00818 146) chain A residue 51-65 type prosite sequence FDDLAERIVQLGHHP description DPS_2 Dps protein family signature 2. FDdLAERivqLGhhP source prosite : PS00819

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