eF-site ID 5ltx-A PDB Code 5ltx Chain A click to enlarge Title LIGAND BINDING DOMAIN OF PSEUDOMONAS AERUGINOSA PAO1 AMINO ACID CHEMORECEPTOR PCTA IN COMPLEX WITH L-MET Classification SIGNALING PROTEIN Compound Chemotaxis protein Source (A0A0H0Z019_PSEAI) Sequence A:  NDYLQRNAIREDLESYLREMGDVTSSNIQNWLGGRLLLVE QTAQTLARDHSPETVSALLEQPALTSTFSFTYLGQQDGVF TMRPDSPMPAGYDPRSRPWYKDAVAAGGLTLTEPYVDAAT QELIITAATPVKAAGNTLGVVGGDLSLKTLVQIINSLDFS GMGYAFLVSGDGKILVHPDKEQVMKTLSEVYPQNTPKIAT GFSEAELHGHTRILAFTPIKGLPSVTWYLALSIDKDKAYA MLS Description Functional site 1) chain A residue 101 type sequence Y description binding site for residue MET A 301 source : AC1 2) chain A residue 121 type sequence Y description binding site for residue MET A 301 source : AC1 3) chain A residue 126 type sequence R description binding site for residue MET A 301 source : AC1 4) chain A residue 128 type sequence W description binding site for residue MET A 301 source : AC1 5) chain A residue 144 type sequence Y description binding site for residue MET A 301 source : AC1 6) chain A residue 146 type sequence D description binding site for residue MET A 301 source : AC1 7) chain A residue 147 type sequence A description binding site for residue MET A 301 source : AC1 8) chain A residue 148 type sequence A description binding site for residue MET A 301 source : AC1 9) chain A residue 173 type sequence D description binding site for residue MET A 301 source : AC1 10) chain A residue 193 type sequence Y description binding site for residue ACT A 302 source : AC2 11) chain A residue 195 type sequence F description binding site for residue ACT A 302 source : AC2 12) chain A residue 206 type sequence H description binding site for residue ACT A 302 source : AC2 13) chain A residue 220 type sequence Y description binding site for residue ACT A 302 source : AC2 14) chain A residue 261 type sequence S description binding site for residue ACT A 302 source : AC2 15) chain A residue 111 type sequence M description binding site for residue ACT A 303 source : AC3 16) chain A residue 112 type sequence R description binding site for residue ACT A 303 source : AC3 17) chain A residue 115 type sequence S description binding site for residue ACT A 303 source : AC3 18) chain A residue 47 type sequence R description binding site for residue GOL A 304 source : AC4 19) chain A residue 230 type sequence G description binding site for residue GOL A 304 source : AC4 20) chain A residue 231 type sequence F description binding site for residue GOL A 304 source : AC4 21) chain A residue 245 type sequence F description binding site for residue GOL A 304 source : AC4 22) chain A residue 246 type sequence T description binding site for residue GOL A 304 source : AC4 23) chain A residue 98 type sequence S description binding site for residue FMT A 306 source : AC6 24) chain A residue 175 type sequence S description binding site for residue FMT A 306 source : AC6 25) chain A residue 178 type sequence T description binding site for residue FMT A 306 source : AC6 26) chain A residue 30 type sequence N description binding site for residue GOL B 301 source : AC7 27) chain A residue 59 type sequence N description binding site for residue GOL B 301 source : AC7 28) chain A residue 62 type sequence G description binding site for residue GOL B 301 source : AC7 29) chain A residue 63 type sequence G description binding site for residue GOL B 301 source : AC7 30) chain A residue 126 type BINDING sequence R description BINDING => ECO:0000269|PubMed:31964737, ECO:0000312|PDB:5T7M source Swiss-Prot : SWS_FT_FI2 31) chain A residue 144 type BINDING sequence Y description BINDING => ECO:0000269|PubMed:31964737, ECO:0000312|PDB:5T7M source Swiss-Prot : SWS_FT_FI2 32) chain A residue 173 type BINDING sequence D description BINDING => ECO:0000269|PubMed:31964737, ECO:0000312|PDB:5T7M source Swiss-Prot : SWS_FT_FI2 33) chain A residue 121 type BINDING sequence Y description BINDING => ECO:0000269|PubMed:31964737, ECO:0000312|PDB:5T7M source Swiss-Prot : SWS_FT_FI2

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