eF-site ID 1kmi-YZ PDB Code 1kmi Chain Y, Z click to enlarge Title CRYSTAL STRUCTURE OF AN E.COLI CHEMOTAXIS PROTEIN, CHEZ Classification SIGNALING PROTEIN Compound Chemotaxis protein cheY Source ORGANISM_SCIENTIFIC: Escherichia coli; Sequence Y:  ADKELKFLVVDDFSTMRRIVRNLLKELGFNNVEEAEDGVD ALNKLQAGGYGFVISDWNMPNMDGLELLKTIRADGAMSAL PVLMVTAEAKKENIIAAAQAGASGYVVKPFTAATLEEKLN KIFEKLGM Z:  SIKPADEHSAGDIIARIGSLTRMLRDSLRELGLDQAIAEA AEAIPDARDRLYYVVQMTAQAAERALNSVEASQPHQDQME KSAKALTQRWDDWFADPIDLADARELVTDTRQFLADVPAH TSFTNAQLLKIMMAQDFQDLTGQVIKRMMDVIQEIERQLL MVLLSQDQVDDLLDSLG Description Functional site 1) chain Y residue 13 type sequence D description BINDING SITE FOR RESIDUE MG Y 301 source : AC1 2) chain Y residue 57 type sequence D description BINDING SITE FOR RESIDUE MG Y 301 source : AC1 3) chain Y residue 59 type sequence N description BINDING SITE FOR RESIDUE MG Y 301 source : AC1 4) chain Z residue 147 type sequence Q description BINDING SITE FOR RESIDUE MG Y 301 source : AC1 5) chain Y residue 57 type sequence D description BINDING SITE FOR RESIDUE BEF Y 201 source : AC2 6) chain Y residue 58 type sequence W description BINDING SITE FOR RESIDUE BEF Y 201 source : AC2 7) chain Y residue 59 type sequence N description BINDING SITE FOR RESIDUE BEF Y 201 source : AC2 8) chain Y residue 87 type sequence T description BINDING SITE FOR RESIDUE BEF Y 201 source : AC2 9) chain Y residue 88 type sequence A description BINDING SITE FOR RESIDUE BEF Y 201 source : AC2 10) chain Z residue 147 type sequence Q description BINDING SITE FOR RESIDUE BEF Y 201 source : AC2 11) chain Z residue 12 type sequence H description BINDING SITE FOR RESIDUE BCN Z 215 source : AC3 12) chain Z residue 39 type sequence Q description BINDING SITE FOR RESIDUE BCN Z 215 source : AC3 13) chain Z residue 98 type sequence F description BINDING SITE FOR RESIDUE BCN Z 215 source : AC3 14) chain Z residue 112 type sequence T description BINDING SITE FOR RESIDUE BCN Z 215 source : AC3 15) chain Y residue 110 type MOD_RES sequence P description N6-acetyllysine => ECO:0000269|PubMed:1390767, ECO:0000269|PubMed:9560203 source Swiss-Prot : SWS_FT_FI5 16) chain Y residue 58 type MOD_RES sequence W description 4-aspartylphosphate => ECO:0000255|PROSITE-ProRule:PRU00169, ECO:0000269|PubMed:1869568, ECO:0000269|PubMed:2689446 source Swiss-Prot : SWS_FT_FI3 17) chain Y residue 93 type MOD_RES sequence E description N6-acetyllysine => ECO:0000269|PubMed:11359578, ECO:0000269|PubMed:9560203 source Swiss-Prot : SWS_FT_FI4 18) chain Y residue 14 type BINDING sequence F description BINDING => ECO:0000269|PubMed:8176739, ECO:0007744|PDB:1CHN source Swiss-Prot : SWS_FT_FI2 19) chain Y residue 58 type BINDING sequence W description BINDING => ECO:0000269|PubMed:8176739, ECO:0007744|PDB:1CHN source Swiss-Prot : SWS_FT_FI2 20) chain Y residue 60 type BINDING sequence M description BINDING => ECO:0000269|PubMed:8176739, ECO:0007744|PDB:1CHN source Swiss-Prot : SWS_FT_FI2 21) chain Z residue 147 type SITE sequence Q description Enhances dephosphorylation of CheY-P source Swiss-Prot : SWS_FT_FI1

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