eF-site ID 6j7m-ACMN PDB Code 6j7m Chain A, C, M, N click to enlarge Title Complex structure of the Pseudomonas aeruginosa rhamnosyltransferase EarP with the acceptor elongation factor EF-P Classification TRANSFERASE Compound Earp Source (EFP_PSEAE) Sequence A:  HMASWDIFCSVVDNYGDIGVTWRLARQLAAEHGQAVRLWV DEPQAFARICPRADPVAHVQCLDGVEVRAWGRPWAPVAAA DVVIEAFACELPEAHRQAMRERKRPSLWLNLEYLSAEEWI GSCHALPSLQACGLSKYFFFPGFREPSGGLLREAGLLERR RRFQASVSAQDEFLASLGVRRKVGERLISLFAYENPALPG WLEQLRDARQPSLLLVPEGRVLADVADWLRVATLAVGDVH VRDALRVQVLPFMAQDDYDRLLWCCDLNAVRGEDSFVRAQ WAGRPLLWHIYRQEEETHLAKLEAFLELYCAGLPADLAEN LRTFWLAWNAGGGLAGAWEGLERQLPEWRREAQRWADEQG MRPDLAARLVQFYADWL C:  HMASWDIFCSVVDNYGDIGVTWRLARQLAAEHGQAVRLWV DEPQAFARICPRADPVAHVQCLDGVEVRAWGRPWAPVAAA DVVIEAFACELPEAHRQAMRERKRPSLWLNLEYLSAEEWI GSCHALPSLQACGLSKYFFFPGFREPSGGLLREAGLLERR RRFQASVSAQDEFLASLGVRRKVGERLISLFAYENPALPG WLEQLRDARQPSLLLVPEGRVLADVADWLRVATLAVGDVH VRDALRVQVLPFMAQDDYDRLLWCCDLNAVRGEDSFVRAQ WAGRPLLWHIYRQEEETHLAKLEAFLELYCAGLPADLAEN LRTFWLAWNAGGGLAGAWEGLERQLPEWRREAQRWADEQG MRPDLAARLVQFYADWL M:  HXKTAQEFRAGQVANINGAPWVIQKAEFNKSGRNAAVVKX KLKNLLTGAGTETVFKADDKLEPIILDRKEVTYSYFADPL YVFXDSEFNQYEIEKDDLEGVLTFIEDGXTDICEAVFYND KVISVELPTTIVRQIAYTEVXKTARLNNGAELQVSAFCEI GDSIEIDTRTGEYKSRVK N:  HXKTAQEFRAGQVANINGAPWVIQKAEFNKSGRNAAVVKX KLKNLLTGAGTETVFKADDKLEPIILDRKEVTYSYFADPL YVFXDSEFNQYEIEKDDLEGVLTFIEDGXTDICEAVFYND KVISVELPTTIVRQIAYTEPXKTARLNNGAELQVSAFCEI GDSIEIDTRTGEYKSRVKA Description Functional site 1) chain A residue 13 type sequence N description binding site for residue TYD A 401 source : AC1 2) chain A residue 14 type sequence Y description binding site for residue TYD A 401 source : AC1 3) chain A residue 15 type sequence G description binding site for residue TYD A 401 source : AC1 4) chain A residue 48 type sequence I description binding site for residue TYD A 401 source : AC1 5) chain A residue 190 type sequence F description binding site for residue TYD A 401 source : AC1 6) chain A residue 192 type sequence Y description binding site for residue TYD A 401 source : AC1 7) chain A residue 251 type sequence F description binding site for residue TYD A 401 source : AC1 8) chain A residue 252 type sequence M description binding site for residue TYD A 401 source : AC1 9) chain A residue 254 type sequence Q description binding site for residue TYD A 401 source : AC1 10) chain A residue 257 type sequence Y description binding site for residue TYD A 401 source : AC1 11) chain A residue 270 type sequence R description binding site for residue TYD A 401 source : AC1 12) chain A residue 271 type sequence G description binding site for residue TYD A 401 source : AC1 13) chain A residue 272 type sequence E description binding site for residue TYD A 401 source : AC1 14) chain A residue 273 type sequence D description binding site for residue TYD A 401 source : AC1 15) chain A residue 274 type sequence S description binding site for residue TYD A 401 source : AC1 16) chain A residue 13 type sequence N description binding site for residue GOL A 402 source : AC2 17) chain A residue 192 type sequence Y description binding site for residue GOL A 402 source : AC2 18) chain A residue 272 type sequence E description binding site for residue GOL A 402 source : AC2 19) chain A residue 290 type sequence Y description binding site for residue GOL A 402 source : AC2 20) chain M residue 32 type sequence R description binding site for residue GOL A 402 source : AC2 21) chain C residue 13 type sequence N description binding site for residue TYD C 401 source : AC3 22) chain C residue 14 type sequence Y description binding site for residue TYD C 401 source : AC3 23) chain C residue 15 type sequence G description binding site for residue TYD C 401 source : AC3 24) chain C residue 48 type sequence I description binding site for residue TYD C 401 source : AC3 25) chain C residue 190 type sequence F description binding site for residue TYD C 401 source : AC3 26) chain C residue 192 type sequence Y description binding site for residue TYD C 401 source : AC3 27) chain C residue 251 type sequence F description binding site for residue TYD C 401 source : AC3 28) chain C residue 252 type sequence M description binding site for residue TYD C 401 source : AC3 29) chain C residue 254 type sequence Q description binding site for residue TYD C 401 source : AC3 30) chain C residue 257 type sequence Y description binding site for residue TYD C 401 source : AC3 31) chain C residue 270 type sequence R description binding site for residue TYD C 401 source : AC3 32) chain C residue 271 type sequence G description binding site for residue TYD C 401 source : AC3 33) chain C residue 272 type sequence E description binding site for residue TYD C 401 source : AC3 34) chain C residue 273 type sequence D description binding site for residue TYD C 401 source : AC3 35) chain C residue 274 type sequence S description binding site for residue TYD C 401 source : AC3 36) chain C residue 15 type sequence G description binding site for residue GOL C 402 source : AC4 37) chain C residue 272 type sequence E description binding site for residue GOL C 402 source : AC4 38) chain C residue 290 type sequence Y description binding site for residue GOL C 402 source : AC4 39) chain N residue 32 type sequence R description binding site for residue GOL C 402 source : AC4 40) chain M residue 32 type CARBOHYD sequence R description N-alpha-linked (Rha) arginine => ECO:0000269|PubMed:26060278, ECO:0000269|PubMed:28451135, ECO:0000269|PubMed:28451332, ECO:0000269|PubMed:31010899 source Swiss-Prot : SWS_FT_FI1 41) chain N residue 32 type CARBOHYD sequence R description N-alpha-linked (Rha) arginine => ECO:0000269|PubMed:26060278, ECO:0000269|PubMed:28451135, ECO:0000269|PubMed:28451332, ECO:0000269|PubMed:31010899 source Swiss-Prot : SWS_FT_FI1 42) chain A residue 272 type ACT_SITE sequence E description ACT_SITE => ECO:0000269|PubMed:31010899 source Swiss-Prot : SWS_FT_FI2 43) chain C residue 272 type ACT_SITE sequence E description ACT_SITE => ECO:0000269|PubMed:31010899 source Swiss-Prot : SWS_FT_FI2 44) chain A residue 13 type BINDING sequence N description BINDING => ECO:0000269|PubMed:31010899, ECO:0007744|PDB:6J7K source Swiss-Prot : SWS_FT_FI3 45) chain A residue 192 type BINDING sequence Y description BINDING => ECO:0000269|PubMed:31010899, ECO:0007744|PDB:6J7K source Swiss-Prot : SWS_FT_FI3 46) chain A residue 252 type BINDING sequence M description BINDING => ECO:0000269|PubMed:31010899, ECO:0007744|PDB:6J7K source Swiss-Prot : SWS_FT_FI3 47) chain A residue 270 type BINDING sequence R description BINDING => ECO:0000269|PubMed:31010899, ECO:0007744|PDB:6J7K source Swiss-Prot : SWS_FT_FI3 48) chain C residue 13 type BINDING sequence N description BINDING => ECO:0000269|PubMed:31010899, ECO:0007744|PDB:6J7K source Swiss-Prot : SWS_FT_FI3 49) chain C residue 192 type BINDING sequence Y description BINDING => ECO:0000269|PubMed:31010899, ECO:0007744|PDB:6J7K source Swiss-Prot : SWS_FT_FI3 50) chain C residue 252 type BINDING sequence M description BINDING => ECO:0000269|PubMed:31010899, ECO:0007744|PDB:6J7K source Swiss-Prot : SWS_FT_FI3 51) chain C residue 270 type BINDING sequence R description BINDING => ECO:0000269|PubMed:31010899, ECO:0007744|PDB:6J7K source Swiss-Prot : SWS_FT_FI3 52) chain A residue 14 type BINDING sequence Y description BINDING => ECO:0000269|PubMed:31010899, ECO:0007744|PDB:6J7L, ECO:0007744|PDB:6J7M source Swiss-Prot : SWS_FT_FI4 53) chain C residue 14 type BINDING sequence Y description BINDING => ECO:0000269|PubMed:31010899, ECO:0007744|PDB:6J7L, ECO:0007744|PDB:6J7M source Swiss-Prot : SWS_FT_FI4

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