eF-site ID 5lt9-AB PDB Code 5lt9 Chain A, B click to enlarge Title Ligand binding domain of Pseudomonas aeruginosa PAO1 amino acid chemoreceptors PctB in complex with L-Arg Classification SIGNALING PROTEIN Compound Methyl-accepting chemotaxis protein PctB Source (A0A0F6UK01_PSEAI) Sequence A:  REDLEDYLHEMGEITASNVQNWLSGRILLIENLAQTLARD HSPETTQALLEQPLLGSTFLFTYLGQTDGTYTARPTSDLP ADYDPRRRPWYNAATSAGQTTLTEPYMEPAIHELVLTIAS PARQGGQPFGVVGGDLSLQTVVKIINSLDFGGMGYAFLVS GDGKILVHPDKDQVMKSLSDVYPRNTPKIGSGFSEAELHG NTRILSFSPVKGLSGLDWYIGISVDKDKAYAMLT B:  EDLEDYLHEMGEITASNVQNWLSGRILLIENLAQTLARDH SPETTQALLEQPLLGSTFLFTYLGQTDGTYTARPTSDLPA DYDPRRRPWYNAATSAGQTTLTEPYMEPAIHELVLTIASP ARQGGQPFGVVGGDLSLQTVVKIINSLDFGGMGYAFLVSG DGKILVHPDKDQVMKSLSDVYPRNTPKIGSGFSEAELHGN TRILSFSPVKGLSGLDWYIGISVDKDKAYAMLTKLRTSDP NSSSVDKLAAALE Description Functional site 1) chain A residue 99 type sequence F description binding site for residue ARG A 301 source : AC1 2) chain A residue 101 type sequence Y description binding site for residue ARG A 301 source : AC1 3) chain A residue 109 type sequence Y description binding site for residue ARG A 301 source : AC1 4) chain A residue 111 type sequence A description binding site for residue ARG A 301 source : AC1 5) chain A residue 113 type sequence P description binding site for residue ARG A 301 source : AC1 6) chain A residue 115 type sequence S description binding site for residue ARG A 301 source : AC1 7) chain A residue 117 type sequence L description binding site for residue ARG A 301 source : AC1 8) chain A residue 121 type sequence Y description binding site for residue ARG A 301 source : AC1 9) chain A residue 126 type sequence R description binding site for residue ARG A 301 source : AC1 10) chain A residue 128 type sequence W description binding site for residue ARG A 301 source : AC1 11) chain A residue 144 type sequence Y description binding site for residue ARG A 301 source : AC1 12) chain A residue 146 type sequence E description binding site for residue ARG A 301 source : AC1 13) chain A residue 147 type sequence P description binding site for residue ARG A 301 source : AC1 14) chain A residue 173 type sequence D description binding site for residue ARG A 301 source : AC1 15) chain A residue 241 type sequence R description binding site for residue NA A 302 source : AC2 16) chain B residue 99 type sequence F description binding site for residue ARG B 301 source : AC3 17) chain B residue 101 type sequence Y description binding site for residue ARG B 301 source : AC3 18) chain B residue 109 type sequence Y description binding site for residue ARG B 301 source : AC3 19) chain B residue 111 type sequence A description binding site for residue ARG B 301 source : AC3 20) chain B residue 115 type sequence S description binding site for residue ARG B 301 source : AC3 21) chain B residue 117 type sequence L description binding site for residue ARG B 301 source : AC3 22) chain B residue 121 type sequence Y description binding site for residue ARG B 301 source : AC3 23) chain B residue 126 type sequence R description binding site for residue ARG B 301 source : AC3 24) chain B residue 128 type sequence W description binding site for residue ARG B 301 source : AC3 25) chain B residue 144 type sequence Y description binding site for residue ARG B 301 source : AC3 26) chain B residue 146 type sequence E description binding site for residue ARG B 301 source : AC3 27) chain B residue 147 type sequence P description binding site for residue ARG B 301 source : AC3 28) chain B residue 148 type sequence A description binding site for residue ARG B 301 source : AC3 29) chain B residue 173 type sequence D description binding site for residue ARG B 301 source : AC3 30) chain B residue 96 type sequence T description binding site for residue GOL B 302 source : AC4 31) chain B residue 97 type sequence F description binding site for residue GOL B 302 source : AC4 32) chain B residue 98 type sequence L description binding site for residue GOL B 302 source : AC4 33) chain B residue 178 type sequence T description binding site for residue GOL B 302 source : AC4 34) chain A residue 109 type BINDING sequence Y description BINDING => ECO:0000269|PubMed:31964737, ECO:0000312|PDB:5LT9 source Swiss-Prot : SWS_FT_FI2 35) chain A residue 146 type BINDING sequence E description BINDING => ECO:0000269|PubMed:31964737, ECO:0000312|PDB:5LT9 source Swiss-Prot : SWS_FT_FI2 36) chain B residue 109 type BINDING sequence Y description BINDING => ECO:0000269|PubMed:31964737, ECO:0000312|PDB:5LT9 source Swiss-Prot : SWS_FT_FI2 37) chain B residue 146 type BINDING sequence E description BINDING => ECO:0000269|PubMed:31964737, ECO:0000312|PDB:5LT9 source Swiss-Prot : SWS_FT_FI2 38) chain B residue 173 type BINDING sequence D description BINDING => ECO:0000269|PubMed:31964737, ECO:0000312|PDB:5LTO source Swiss-Prot : SWS_FT_FI3 39) chain B residue 121 type BINDING sequence Y description BINDING => ECO:0000269|PubMed:31964737, ECO:0000312|PDB:5LTO source Swiss-Prot : SWS_FT_FI3 40) chain B residue 126 type BINDING sequence R description BINDING => ECO:0000269|PubMed:31964737, ECO:0000312|PDB:5LTO source Swiss-Prot : SWS_FT_FI3 41) chain B residue 144 type BINDING sequence Y description BINDING => ECO:0000269|PubMed:31964737, ECO:0000312|PDB:5LTO source Swiss-Prot : SWS_FT_FI3 42) chain A residue 115 type BINDING sequence S description BINDING => ECO:0000269|PubMed:31964737, ECO:0000312|PDB:5LTO source Swiss-Prot : SWS_FT_FI3 43) chain A residue 121 type BINDING sequence Y description BINDING => ECO:0000269|PubMed:31964737, ECO:0000312|PDB:5LTO source Swiss-Prot : SWS_FT_FI3 44) chain A residue 126 type BINDING sequence R description BINDING => ECO:0000269|PubMed:31964737, ECO:0000312|PDB:5LTO source Swiss-Prot : SWS_FT_FI3 45) chain A residue 144 type BINDING sequence Y description BINDING => ECO:0000269|PubMed:31964737, ECO:0000312|PDB:5LTO source Swiss-Prot : SWS_FT_FI3 46) chain A residue 173 type BINDING sequence D description BINDING => ECO:0000269|PubMed:31964737, ECO:0000312|PDB:5LTO source Swiss-Prot : SWS_FT_FI3 47) chain B residue 115 type BINDING sequence S description BINDING => ECO:0000269|PubMed:31964737, ECO:0000312|PDB:5LTO source Swiss-Prot : SWS_FT_FI3

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