eF-site ID 1ffw-ABCD PDB Code 1ffw Chain A, B, C, D click to enlarge Title CHEY-BINDING DOMAIN OF CHEA IN COMPLEX WITH CHEY WITH A BOUND IMIDO DIPHOSPHATE Classification TRANSFERASE/SIGNALING PROTEIN Compound CHEMOTAXIS PROTEIN CHEY Source null (CHEA_ECOLI) Sequence A:  ADKELKFLVVDDFSTMRRIVRNLLKELGFNNVEEAEDGVD ALNKLQAGGYGFVISDWNMPNMDGLELLKTIRADGAMSAL PVLMVTAEAKKENIIAAAQAGASGYVVKPFTAATLEEKLN KIFEKLGM B:  ARRIILSRLKAGEVDLLEEELGHLTTLTDVVKGADSLSAI LPGDIAEDDITAVLCFVIEADQITFETV C:  ADKELKFLVVDDFSTMRRIVRNLLKELGFNNVEEAEDGVD ALNKLQAGGYGFVISDWNMPNMDGLELLKTIRADGAMSAL PVLMVTAEAKKENIIAAAQAGASGYVVKPFTAATLEEKLN KIFEKLGM D:  ARRIILSRLKAGEVDLLEEELGHLTTLTDVVKGADSLSAI LPGDIAEDDITAVLCFVIEADQITFETV Description Functional site 1) chain A residue 12 type sequence D description BINDING SITE FOR RESIDUE MN A 1 source : AC1 2) chain A residue 13 type sequence D description BINDING SITE FOR RESIDUE MN A 1 source : AC1 3) chain A residue 57 type sequence D description BINDING SITE FOR RESIDUE MN A 1 source : AC1 4) chain A residue 59 type sequence N description BINDING SITE FOR RESIDUE MN A 1 source : AC1 5) chain C residue 5 type sequence E description BINDING SITE FOR RESIDUE MN A 1 source : AC1 6) chain C residue 12 type sequence D description BINDING SITE FOR RESIDUE MN C 130 source : AC2 7) chain C residue 13 type sequence D description BINDING SITE FOR RESIDUE MN C 130 source : AC2 8) chain C residue 57 type sequence D description BINDING SITE FOR RESIDUE MN C 130 source : AC2 9) chain C residue 59 type sequence N description BINDING SITE FOR RESIDUE MN C 130 source : AC2 10) chain A residue 13 type sequence D description BINDING SITE FOR RESIDUE PON A 330 source : AC3 11) chain A residue 14 type sequence F description BINDING SITE FOR RESIDUE PON A 330 source : AC3 12) chain A residue 15 type sequence S description BINDING SITE FOR RESIDUE PON A 330 source : AC3 13) chain A residue 109 type MOD_RES sequence K description N6-acetyllysine => ECO:0000269|PubMed:1390767, ECO:0000269|PubMed:9560203 source Swiss-Prot : SWS_FT_FI5 14) chain C residue 109 type MOD_RES sequence K description N6-acetyllysine => ECO:0000269|PubMed:1390767, ECO:0000269|PubMed:9560203 source Swiss-Prot : SWS_FT_FI5 15) chain C residue 12 type BINDING sequence D description BINDING => ECO:0000250|UniProtKB:A0A0H3AMJ9 source Swiss-Prot : SWS_FT_FI1 16) chain A residue 12 type BINDING sequence D description BINDING => ECO:0000250|UniProtKB:A0A0H3AMJ9 source Swiss-Prot : SWS_FT_FI1 17) chain A residue 59 type BINDING sequence N description BINDING => ECO:0000269|PubMed:8176739, ECO:0007744|PDB:1CHN source Swiss-Prot : SWS_FT_FI2 18) chain C residue 13 type BINDING sequence D description BINDING => ECO:0000269|PubMed:8176739, ECO:0007744|PDB:1CHN source Swiss-Prot : SWS_FT_FI2 19) chain C residue 57 type BINDING sequence D description BINDING => ECO:0000269|PubMed:8176739, ECO:0007744|PDB:1CHN source Swiss-Prot : SWS_FT_FI2 20) chain C residue 59 type BINDING sequence N description BINDING => ECO:0000269|PubMed:8176739, ECO:0007744|PDB:1CHN source Swiss-Prot : SWS_FT_FI2 21) chain A residue 57 type BINDING sequence D description BINDING => ECO:0000269|PubMed:8176739, ECO:0007744|PDB:1CHN source Swiss-Prot : SWS_FT_FI2 22) chain A residue 13 type BINDING sequence D description BINDING => ECO:0000269|PubMed:8176739, ECO:0007744|PDB:1CHN source Swiss-Prot : SWS_FT_FI2 23) chain A residue 57 type MOD_RES sequence D description 4-aspartylphosphate => ECO:0000255|PROSITE-ProRule:PRU00169, ECO:0000269|PubMed:1869568, ECO:0000269|PubMed:2689446 source Swiss-Prot : SWS_FT_FI3 24) chain C residue 57 type MOD_RES sequence D description 4-aspartylphosphate => ECO:0000255|PROSITE-ProRule:PRU00169, ECO:0000269|PubMed:1869568, ECO:0000269|PubMed:2689446 source Swiss-Prot : SWS_FT_FI3 25) chain A residue 92 type MOD_RES sequence K description N6-acetyllysine => ECO:0000269|PubMed:11359578, ECO:0000269|PubMed:9560203 source Swiss-Prot : SWS_FT_FI4 26) chain C residue 92 type MOD_RES sequence K description N6-acetyllysine => ECO:0000269|PubMed:11359578, ECO:0000269|PubMed:9560203 source Swiss-Prot : SWS_FT_FI4

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