eF-site ID 5ya2-ABCD PDB Code 5ya2 Chain A, B, C, D click to enlarge Title Crystal structure of LsrK-HPr complex with ADP Classification STRUCTURAL PROTEIN Compound Autoinducer-2 kinase Source (PTHP_ECOLI) Sequence A:  SKYYLMALDAGTGSIRAVIFDLEGNQIAVGQAEWRHMEFD LNKNWQLACECMRQALHNAGIAPEYIAAVSACSMREGIVL YNNEGAPIWACANVDARAAREVSELKELHNNTFENEVYRA TGQTLALSAIPRLLWLAHHRSDIYRQASTITMISDWLAYM LSGELAVDPSNAGTTGLLDLTTRDWKPALLDMAGLRADIL SPVKETGTLLGVVSSQAAELCGLKAGTPVVVGGGDVQLGC LGLGVVRPAQTAVLGGTFWQQVVNLAAPVTDPEMNVRVNP HVIPGMVQAESISFFTGLTMRWFRDAFCAEEKLIAERLGI DTYTLLEEMASRVPPGSWGVMPIFSDHAAPSFINLSIDPD KCNKATLFRALEENAAIVSACNLQQIADFSNIHPSSLVFA GGGSKGKLWSQILADVSGLPVNIPVVKEATALGCAIAAGV GAGIFSSMAETGERLVRWERTHTPDPEKHELYQDSRDK B:  SKYYLMALDAGTGSIRAVIFDLEGNQIAVGQAEWRHMEFD LNKNWQLACECMRQALHNAGIAPEYIAAVSACSMREGIVL YNNEGAPIWACANVDARAAREVSELKELHNNTFENEVYRA TGQTLALSAIPRLLWLAHHRSDIYRQASTITMISDWLAYM LSGELAVDPSNAGTTGLLDLTTRDWKPALLDMAGLRADIL SPVKETGTLLGVVSSQAAELCGLKAGTPVVVGGGDVQLGC LGLGVVRPAQTAVLGGTFWQQVVNLAAPVTDPEMNVRVNP HVIPGMVQAESISFFTGLTMRWFRDAFCAEEKLIAERLGI DTYTLLEEMASRVPPGSWGVMPIFSDHAAPSFINLSIDPD KCNKATLFRALEENAAIVSACNLQQIADFSNIHPSSLVFA GGGSKGKLWSQILADVSGLPVNIPVVKEATALGCAIAAGV GAGIFSSMAETGERLVRWERTHTPDPEKHELYQDSRDK C:  MFQQEVTITAPNGLHTRPAAQFVKEAKGFTSEITVTSNGK SASAKSLFKLQTLGLTQGTVVTISAEGEDEQKAVEHLVKL MAELE D:  MFQQEVTITAPNGLHTRPAAQFVKEAKGFTSEITVTSNGK SASAKSLFKLQTLGLTQGTVVTISAEGEDEQKAVEHLVKL MAELE Description Functional site 1) chain A residue 315 type sequence G description binding site for residue ADP A 601 source : AC1 2) chain A residue 318 type sequence M description binding site for residue ADP A 601 source : AC1 3) chain A residue 319 type sequence R description binding site for residue ADP A 601 source : AC1 4) chain A residue 322 type sequence R description binding site for residue ADP A 601 source : AC1 5) chain A residue 341 type sequence Y description binding site for residue ADP A 601 source : AC1 6) chain A residue 428 type sequence G description binding site for residue ADP A 601 source : AC1 7) chain A residue 432 type sequence G description binding site for residue ADP A 601 source : AC1 8) chain A residue 127 type sequence H description binding site for residue HEZ A 602 source : AC2 9) chain A residue 131 type sequence F description binding site for residue HEZ A 602 source : AC2 10) chain A residue 134 type sequence E description binding site for residue HEZ A 602 source : AC2 11) chain A residue 206 type sequence A description binding site for residue HEZ A 602 source : AC2 12) chain A residue 210 type sequence M description binding site for residue HEZ A 602 source : AC2 13) chain A residue 204 type sequence K description binding site for residue PO4 A 603 source : AC3 14) chain B residue 204 type sequence K description binding site for residue PO4 A 603 source : AC3 15) chain A residue 127 type sequence H description binding site for residue PO4 A 604 source : AC4 16) chain C residue 24 type sequence K description binding site for residue PO4 A 604 source : AC4 17) chain A residue 197 type sequence D description binding site for residue PO4 A 605 source : AC5 18) chain A residue 204 type sequence K description binding site for residue PO4 A 605 source : AC5 19) chain B residue 197 type sequence D description binding site for residue PO4 A 605 source : AC5 20) chain B residue 204 type sequence K description binding site for residue PO4 A 605 source : AC5 21) chain B residue 315 type sequence G description binding site for residue ADP B 701 source : AC6 22) chain B residue 319 type sequence R description binding site for residue ADP B 701 source : AC6 23) chain B residue 322 type sequence R description binding site for residue ADP B 701 source : AC6 24) chain B residue 341 type sequence Y description binding site for residue ADP B 701 source : AC6 25) chain B residue 428 type sequence G description binding site for residue ADP B 701 source : AC6 26) chain B residue 432 type sequence G description binding site for residue ADP B 701 source : AC6 27) chain B residue 127 type sequence H description binding site for residue HEZ B 702 source : AC7 28) chain B residue 134 type sequence E description binding site for residue HEZ B 702 source : AC7 29) chain B residue 206 type sequence A description binding site for residue HEZ B 702 source : AC7 30) chain B residue 210 type sequence M description binding site for residue HEZ B 702 source : AC7 31) chain D residue 23 type sequence V description binding site for residue HEZ B 702 source : AC7 32) chain B residue 127 type sequence H description binding site for residue PO4 B 703 source : AC8 33) chain D residue 24 type sequence K description binding site for residue PO4 B 703 source : AC8 34) chain C residue 38 type sequence N description binding site for residue PO4 C 101 source : AC9 35) chain C residue 40 type sequence K description binding site for residue PO4 C 101 source : AC9 36) chain D residue 38 type sequence N description binding site for residue PO4 D 101 source : AD1 37) chain D residue 40 type sequence K description binding site for residue PO4 D 101 source : AD1 38) chain C residue 13-20 type prosite sequence GLHTRPAA description PTS_HPR_HIS PTS HPR domain histidine phosphorylation site signature. GLHTRPAA source prosite : PS00369 39) chain C residue 39-54 type prosite sequence GKSASAKSLFKLQTLG description PTS_HPR_SER PTS HPR domain serine phosphorylation site signature. GKsASaKSLFKLQtLG source prosite : PS00589 40) chain C residue 15 type ACT_SITE sequence H description Pros-phosphohistidine intermediate => ECO:0000255|PROSITE-ProRule:PRU00681, ECO:0000269|PubMed:2261470 source Swiss-Prot : SWS_FT_FI1 41) chain D residue 15 type ACT_SITE sequence H description Pros-phosphohistidine intermediate => ECO:0000255|PROSITE-ProRule:PRU00681, ECO:0000269|PubMed:2261470 source Swiss-Prot : SWS_FT_FI1

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