eF-site ID 6hb5-AB PDB Code 6hb5 Chain A, B click to enlarge Title Crystal structure of E. coli tyrRS in complex with 5'-O-(N-L-tyrosyl)sulfamoyl-cytidine Classification LIGASE Compound Tyrosine--tRNA ligase Source (A0A140NBN7_ECOBD) Sequence A:  NLIKQLQERGLVAQVTDEEALAERLAQGPIALYCGFDPTA DSLHLGHLVPLLCLKRFQQAGHKPVALVGGATGLIGDPSF KAAERKLNTEETVQEWVDKIRKQVAPFLDFDCGENSAIAA NNYDWFGNMNVLTFLRDIGKHFSVNQMINKEAVKQRLNRE DQGISFTEFSYNLLQGYDFACLNKQYGVVLQIGGSDQWGN ITSGIDLTRRLHQNQVFGLTVPLITKADGTKFGKTEGGAV WLDPKKTSPYKFYQFWINTADADVYRFLKFFTFMSIEEIN ALEEEPRAQYVLAEQVTRLVHGEEGLQAAKRITECLFSGS LSALSEADFEQLAQDGVPMVEMEKGADLMQALVDSELQPS RGQARKTIASNAITINGEKQSDPEYFFKEEERLFGRFTLL RRGKKNYCLICWK B:  NLIKQLQERGLVAQVTDEEALAERLAQGPIALYCGFDPTA DSLHLGHLVPLLCLKRFQQAGHKPVALVGGATGLIGDPSF KAAERKLNTEETVQEWVDKIRKQVAPFLDFDCGENSAIAA NNYDWFGNMNVLTFLRDIGKHFSVNQMINKEAVKQRLNRE DQGISFTEFSYNLLQGYDFACLNKQYGVVLQIGGSDQWGN ITSGIDLTRRLHQNQVFGLTVPLITKADGTKFGKTAVWLD PKKTSPYKFYQFWINTADADVYRFLKFFTFMSIEEINALE EEDKNSGKAPRAQYVLAEQVTRLVHGEEGLQAAKRITECL FSGSLSALSEADFEQLAQDGVPMVEMEKGADLMQALVDSE LQPSRGQARKTIASNAITINGEKQSDPEYFFKEEERLFGR FTLLRRGKKNYCLICWK Description (1)  Tyrosine--tRNA ligase (E.C.6.1.1.1) Functional site 1) chain A residue 37 type sequence Y description binding site for residue YSC A 501 source : AC1 2) chain A residue 39 type sequence G description binding site for residue YSC A 501 source : AC1 3) chain A residue 41 type sequence D description binding site for residue YSC A 501 source : AC1 4) chain A residue 50 type sequence G description binding site for residue YSC A 501 source : AC1 5) chain A residue 51 type sequence H description binding site for residue YSC A 501 source : AC1 6) chain A residue 54 type sequence P description binding site for residue YSC A 501 source : AC1 7) chain A residue 71 type sequence L description binding site for residue YSC A 501 source : AC1 8) chain A residue 76 type sequence T description binding site for residue YSC A 501 source : AC1 9) chain A residue 81 type sequence D description binding site for residue YSC A 501 source : AC1 10) chain A residue 175 type sequence Y description binding site for residue YSC A 501 source : AC1 11) chain A residue 179 type sequence Q description binding site for residue YSC A 501 source : AC1 12) chain A residue 182 type sequence D description binding site for residue YSC A 501 source : AC1 13) chain A residue 195 type sequence Q description binding site for residue YSC A 501 source : AC1 14) chain A residue 197 type sequence G description binding site for residue YSC A 501 source : AC1 15) chain A residue 198 type sequence G description binding site for residue YSC A 501 source : AC1 16) chain A residue 200 type sequence D description binding site for residue YSC A 501 source : AC1 17) chain A residue 201 type sequence Q description binding site for residue YSC A 501 source : AC1 18) chain A residue 227 type sequence L description binding site for residue YSC A 501 source : AC1 19) chain A residue 33 type sequence P description binding site for residue EDO A 502 source : AC2 20) chain A residue 110 type sequence P description binding site for residue EDO A 503 source : AC3 21) chain A residue 111 type sequence F description binding site for residue EDO A 503 source : AC3 22) chain A residue 310 type sequence L description binding site for residue EDO A 503 source : AC3 23) chain A residue 386 type sequence I description binding site for residue EDO A 504 source : AC4 24) chain A residue 389 type sequence E description binding site for residue EDO A 504 source : AC4 25) chain A residue 390 type sequence K description binding site for residue EDO A 504 source : AC4 26) chain A residue 391 type sequence Q description binding site for residue EDO A 504 source : AC4 27) chain A residue 396 type sequence Y description binding site for residue EDO A 504 source : AC4 28) chain A residue 402 type sequence E description binding site for residue EDO A 504 source : AC4 29) chain A residue 398 type sequence F description binding site for residue CL A 505 source : AC5 30) chain A residue 403 type sequence R description binding site for residue CL A 505 source : AC5 31) chain B residue 37 type sequence Y description binding site for residue YSC B 501 source : AC6 32) chain B residue 39 type sequence G description binding site for residue YSC B 501 source : AC6 33) chain B residue 41 type sequence D description binding site for residue YSC B 501 source : AC6 34) chain B residue 50 type sequence G description binding site for residue YSC B 501 source : AC6 35) chain B residue 51 type sequence H description binding site for residue YSC B 501 source : AC6 36) chain B residue 54 type sequence P description binding site for residue YSC B 501 source : AC6 37) chain B residue 71 type sequence L description binding site for residue YSC B 501 source : AC6 38) chain B residue 76 type sequence T description binding site for residue YSC B 501 source : AC6 39) chain B residue 81 type sequence D description binding site for residue YSC B 501 source : AC6 40) chain B residue 175 type sequence Y description binding site for residue YSC B 501 source : AC6 41) chain B residue 179 type sequence Q description binding site for residue YSC B 501 source : AC6 42) chain B residue 182 type sequence D description binding site for residue YSC B 501 source : AC6 43) chain B residue 195 type sequence Q description binding site for residue YSC B 501 source : AC6 44) chain B residue 197 type sequence G description binding site for residue YSC B 501 source : AC6 45) chain B residue 198 type sequence G description binding site for residue YSC B 501 source : AC6 46) chain B residue 200 type sequence D description binding site for residue YSC B 501 source : AC6 47) chain B residue 201 type sequence Q description binding site for residue YSC B 501 source : AC6 48) chain B residue 227 type sequence L description binding site for residue YSC B 501 source : AC6 49) chain A residue 37 type BINDING sequence Y description BINDING => ECO:0000255|HAMAP-Rule:MF_02006, ECO:0000269|PubMed:15663931, ECO:0000305|PubMed:15671170 source Swiss-Prot : SWS_FT_FI1 50) chain B residue 37 type BINDING sequence Y description BINDING => ECO:0000255|HAMAP-Rule:MF_02006, ECO:0000269|PubMed:15663931, ECO:0000305|PubMed:15671170 source Swiss-Prot : SWS_FT_FI1 51) chain A residue 175 type BINDING sequence Y description BINDING => ECO:0000255|HAMAP-Rule:MF_02006, ECO:0000269|PubMed:15663931, ECO:0000269|PubMed:15671170, ECO:0000305|PubMed:20159998 source Swiss-Prot : SWS_FT_FI2 52) chain A residue 179 type BINDING sequence Q description BINDING => ECO:0000255|HAMAP-Rule:MF_02006, ECO:0000269|PubMed:15663931, ECO:0000269|PubMed:15671170, ECO:0000305|PubMed:20159998 source Swiss-Prot : SWS_FT_FI2 53) chain B residue 175 type BINDING sequence Y description BINDING => ECO:0000255|HAMAP-Rule:MF_02006, ECO:0000269|PubMed:15663931, ECO:0000269|PubMed:15671170, ECO:0000305|PubMed:20159998 source Swiss-Prot : SWS_FT_FI2 54) chain B residue 179 type BINDING sequence Q description BINDING => ECO:0000255|HAMAP-Rule:MF_02006, ECO:0000269|PubMed:15663931, ECO:0000269|PubMed:15671170, ECO:0000305|PubMed:20159998 source Swiss-Prot : SWS_FT_FI2 55) chain A residue 238 type BINDING sequence K description BINDING => ECO:0000255|HAMAP-Rule:MF_02006 source Swiss-Prot : SWS_FT_FI3 56) chain B residue 238 type BINDING sequence K description BINDING => ECO:0000255|HAMAP-Rule:MF_02006 source Swiss-Prot : SWS_FT_FI3 57) chain A residue 231 type SITE sequence A description Cross-linked with tRNA by periodate oxidation source Swiss-Prot : SWS_FT_FI4 58) chain A residue 238 type SITE sequence K description Cross-linked with tRNA by periodate oxidation source Swiss-Prot : SWS_FT_FI4 59) chain B residue 231 type SITE sequence A description Cross-linked with tRNA by periodate oxidation source Swiss-Prot : SWS_FT_FI4 60) chain B residue 238 type SITE sequence K description Cross-linked with tRNA by periodate oxidation source Swiss-Prot : SWS_FT_FI4 61) chain A residue 235 type SITE sequence K description Cross-linked with tRNA by periodate oxidation; predominant source Swiss-Prot : SWS_FT_FI5 62) chain B residue 235 type SITE sequence K description Cross-linked with tRNA by periodate oxidation; predominant source Swiss-Prot : SWS_FT_FI5 63) chain A residue 42-52 type prosite sequence PTADSLHLGHL description AA_TRNA_LIGASE_I Aminoacyl-transfer RNA synthetases class-I signature. Pt.ADsLHLGHL source prosite : PS00178 64) chain A residue 144 type MOD_RES sequence K description N6-acetyllysine => ECO:0000269|PubMed:18723842 source Swiss-Prot : SWS_FT_FI6 65) chain B residue 144 type MOD_RES sequence K description N6-acetyllysine => ECO:0000269|PubMed:18723842 source Swiss-Prot : SWS_FT_FI6

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