eF-site ID 6hb7-AB
PDB Code 6hb7
Chain A, B

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Title Crystal structure of E. coli tyrRS in complex with 5'-O-(N-L-tyrosyl)sulfamoyl-N3-methyluridine
Classification LIGASE
Compound Tyrosine--tRNA ligase
Source (A0A140NBN7_ECOBD)
Sequence A:  NLIKQLQERGLVAQVTDEEALAERLAQGPIALYCGFDPTA
DSLHLGHLVPLLCLKRFQQAGHKPVALVGGATGLIGDPSF
KAAERKLNTEETVQEWVDKIRKQVAPFLDFDCGENSAIAA
NNYDWFGNMNVLTFLRDIGKHFSVNQMINKEAVKQRLNRE
DQGISFTEFSYNLLQGYDFACLNKQYGVVLQIGGSDQWGN
ITSGIDLTRRLHQNQVFGLTVPLITKADGTKFGKAVWLDP
KKTSPYKFYQFWINTADADVYRFLKFFTFMSIEEINALEE
EDKNRAQYVLAEQVTRLVHGEEGLQAAKRITECLFSGSLS
ALSEADFEQLAQDGVPMVEMEKGADLMQALVDSELQPSRG
QARKTIASNAITINGEKQSDPEYFFKEEERLFGRFTLLRR
GKKNYCLICWK
B:  SNLIKQLQERGLVAQVTDEEALAERLAQGPIALYCGFDPT
ADSLHLGHLVPLLCLKRFQQAGHKPVALVGGATGLIGDPS
FKAAERKLNTEETVQEWVDKIRKQVAPFLDFDCGENSAIA
ANNYDWFGNMNVLTFLRDIGKHFSVNQMINKEAVKQRLNR
EDQGISFTEFSYNLLQGYDFACLNKQYGVVLQIGGSDQWG
NITSGIDLTRRLHQNQVFGLTVPLITKADGTAVWLDPKKT
SPYKFYQFWINTADADVYRFLKFFTFMSIEEINALEEEDK
NSGKAPRAQYVLAEQVTRLVHGEEGLQAAKRITECLFSGS
LSALSEADFEQLAQDGVPMVEMEKGADLMQALVDSELQPS
RGQARKTIASNAITINGEKQSDPEYFFKEEERLFGRFTLL
RRGKKNYCLICWK
Description (1)  tyrosyl-tRNA synthetase


Functional site

1) chain A
residue 37
type
sequence Y
description binding site for residue Y3U A 501
source : AC1

2) chain A
residue 39
type
sequence G
description binding site for residue Y3U A 501
source : AC1

3) chain A
residue 41
type
sequence D
description binding site for residue Y3U A 501
source : AC1

4) chain A
residue 50
type
sequence G
description binding site for residue Y3U A 501
source : AC1

5) chain A
residue 51
type
sequence H
description binding site for residue Y3U A 501
source : AC1

6) chain A
residue 54
type
sequence P
description binding site for residue Y3U A 501
source : AC1

7) chain A
residue 71
type
sequence L
description binding site for residue Y3U A 501
source : AC1

8) chain A
residue 76
type
sequence T
description binding site for residue Y3U A 501
source : AC1

9) chain A
residue 81
type
sequence D
description binding site for residue Y3U A 501
source : AC1

10) chain A
residue 175
type
sequence Y
description binding site for residue Y3U A 501
source : AC1

11) chain A
residue 179
type
sequence Q
description binding site for residue Y3U A 501
source : AC1

12) chain A
residue 182
type
sequence D
description binding site for residue Y3U A 501
source : AC1

13) chain A
residue 195
type
sequence Q
description binding site for residue Y3U A 501
source : AC1

14) chain A
residue 197
type
sequence G
description binding site for residue Y3U A 501
source : AC1

15) chain A
residue 198
type
sequence G
description binding site for residue Y3U A 501
source : AC1

16) chain A
residue 200
type
sequence D
description binding site for residue Y3U A 501
source : AC1

17) chain A
residue 201
type
sequence Q
description binding site for residue Y3U A 501
source : AC1

18) chain A
residue 225
type
sequence V
description binding site for residue Y3U A 501
source : AC1

19) chain A
residue 227
type
sequence L
description binding site for residue Y3U A 501
source : AC1

20) chain A
residue 34
type
sequence I
description binding site for residue EDO A 502
source : AC2

21) chain A
residue 118
type
sequence E
description binding site for residue EDO A 502
source : AC2

22) chain A
residue 105
type
sequence R
description binding site for residue EDO A 503
source : AC3

23) chain A
residue 123
type
sequence A
description binding site for residue EDO A 503
source : AC3

24) chain A
residue 124
type
sequence A
description binding site for residue EDO A 503
source : AC3

25) chain A
residue 125
type
sequence N
description binding site for residue EDO A 503
source : AC3

26) chain A
residue 128
type
sequence D
description binding site for residue EDO A 503
source : AC3

27) chain A
residue 386
type
sequence I
description binding site for residue EDO A 504
source : AC4

28) chain A
residue 389
type
sequence E
description binding site for residue EDO A 504
source : AC4

29) chain A
residue 390
type
sequence K
description binding site for residue EDO A 504
source : AC4

30) chain A
residue 391
type
sequence Q
description binding site for residue EDO A 504
source : AC4

31) chain A
residue 396
type
sequence Y
description binding site for residue EDO A 504
source : AC4

32) chain A
residue 402
type
sequence E
description binding site for residue EDO A 504
source : AC4

33) chain A
residue 398
type
sequence F
description binding site for residue CL A 505
source : AC5

34) chain A
residue 403
type
sequence R
description binding site for residue CL A 505
source : AC5

35) chain B
residue 37
type
sequence Y
description binding site for residue Y3U B 501
source : AC6

36) chain B
residue 39
type
sequence G
description binding site for residue Y3U B 501
source : AC6

37) chain B
residue 41
type
sequence D
description binding site for residue Y3U B 501
source : AC6

38) chain B
residue 50
type
sequence G
description binding site for residue Y3U B 501
source : AC6

39) chain B
residue 51
type
sequence H
description binding site for residue Y3U B 501
source : AC6

40) chain B
residue 54
type
sequence P
description binding site for residue Y3U B 501
source : AC6

41) chain B
residue 71
type
sequence L
description binding site for residue Y3U B 501
source : AC6

42) chain B
residue 76
type
sequence T
description binding site for residue Y3U B 501
source : AC6

43) chain B
residue 81
type
sequence D
description binding site for residue Y3U B 501
source : AC6

44) chain B
residue 175
type
sequence Y
description binding site for residue Y3U B 501
source : AC6

45) chain B
residue 179
type
sequence Q
description binding site for residue Y3U B 501
source : AC6

46) chain B
residue 182
type
sequence D
description binding site for residue Y3U B 501
source : AC6

47) chain B
residue 195
type
sequence Q
description binding site for residue Y3U B 501
source : AC6

48) chain B
residue 197
type
sequence G
description binding site for residue Y3U B 501
source : AC6

49) chain B
residue 198
type
sequence G
description binding site for residue Y3U B 501
source : AC6

50) chain B
residue 200
type
sequence D
description binding site for residue Y3U B 501
source : AC6

51) chain B
residue 201
type
sequence Q
description binding site for residue Y3U B 501
source : AC6

52) chain B
residue 225
type
sequence V
description binding site for residue Y3U B 501
source : AC6

53) chain B
residue 226
type
sequence P
description binding site for residue Y3U B 501
source : AC6

54) chain B
residue 227
type
sequence L
description binding site for residue Y3U B 501
source : AC6

55) 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

56) 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

57) 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

58) 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

59) 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

60) 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

61) chain A
residue 238
type BINDING
sequence K
description BINDING => ECO:0000255|HAMAP-Rule:MF_02006
source Swiss-Prot : SWS_FT_FI3

62) chain A
residue 144
type MOD_RES
sequence K
description N6-acetyllysine => ECO:0000269|PubMed:18723842
source Swiss-Prot : SWS_FT_FI6

63) chain B
residue 144
type MOD_RES
sequence K
description N6-acetyllysine => ECO:0000269|PubMed:18723842
source Swiss-Prot : SWS_FT_FI6

64) chain A
residue 231
type SITE
sequence A
description Cross-linked with tRNA by periodate oxidation
source Swiss-Prot : SWS_FT_FI4

65) chain A
residue 238
type SITE
sequence K
description Cross-linked with tRNA by periodate oxidation
source Swiss-Prot : SWS_FT_FI4

66) chain B
residue 231
type SITE
sequence A
description Cross-linked with tRNA by periodate oxidation
source Swiss-Prot : SWS_FT_FI4

67) chain A
residue 235
type SITE
sequence K
description Cross-linked with tRNA by periodate oxidation; predominant
source Swiss-Prot : SWS_FT_FI5

68) 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


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