eF-site ID 1asz-B
PDB Code 1asz
Chain B

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Title THE ACTIVE SITE OF YEAST ASPARTYL-TRNA SYNTHETASE: STRUCTURAL AND FUNCTIONAL ASPECTS OF THE AMINOACYLATION REACTION
Classification COMPLEX (AMINOACYL-TRNA SYNTHASE/TRNA)
Compound T-RNA (75-MER)
Source (1ASZ)
Sequence B:  EDTAKDNYGKLPLIQSRDSDRTGQKRVKFVDLDEAKDSDK
EVLFRARVHNTRQQGATLAFLTLRQQASLIQGLVKANKEG
TISKNMVKWAGSLNLESIVLVRGIVKKVDEPIKSATVQNL
EIHITKIYTISETPEALPILLEDASRSEAEAEAAGLPVVN
LDTRLDYRVIDLRTVTNQAIFRIQAGVCELFREYLATKKF
TEVHTPKLLGAPSEGGSSVFEVTYFKGKAYLAQSPQFNKQ
QLIVADFERVYEIGPVFRAENSNTHRHMTEFTGLDMEMAF
EEHYHEVLDTLSELFVFIFSELPKRFAHEIELVRKQYPVE
EFKLPKDGKMVRLTYKEGIEMLRAAGKEIGDFEDLSTENE
KFLGKLVRDKYDTDFYILDKFPLEIRPFYTMPDPANPKYS
NSYDFFMRGEEILSGAQRIHDHALLQERMKAHGLSPEDPG
LKDYCDGFSYGCPPHAGGGIGLERVVMFYLDLKNIRRASL
FPRDPKRLRP
Description


Functional site

1) chain B
residue 325
type
sequence R
description BINDING SITE FOR RESIDUE ATP B 701
source : AC2

2) chain B
residue 335
type
sequence M
description BINDING SITE FOR RESIDUE ATP B 701
source : AC2

3) chain B
residue 338
type
sequence F
description BINDING SITE FOR RESIDUE ATP B 701
source : AC2

4) chain B
residue 478
type
sequence E
description BINDING SITE FOR RESIDUE ATP B 701
source : AC2

5) chain B
residue 479
type
sequence I
description BINDING SITE FOR RESIDUE ATP B 701
source : AC2

6) chain B
residue 480
type
sequence L
description BINDING SITE FOR RESIDUE ATP B 701
source : AC2

7) chain B
residue 481
type
sequence S
description BINDING SITE FOR RESIDUE ATP B 701
source : AC2

8) chain B
residue 527
type
sequence I
description BINDING SITE FOR RESIDUE ATP B 701
source : AC2

9) chain B
residue 531
type
sequence R
description BINDING SITE FOR RESIDUE ATP B 701
source : AC2

10) chain B
residue 326
type catalytic
sequence A
description 404
source MCSA : MCSA2

11) chain B
residue 328
type catalytic
sequence N
description 404
source MCSA : MCSA2

12) chain B
residue 334
type catalytic
sequence H
description 404
source MCSA : MCSA2

13) chain B
residue 335
type catalytic
sequence M
description 404
source MCSA : MCSA2

14) chain B
residue 479
type catalytic
sequence I
description 404
source MCSA : MCSA2

15) chain B
residue 482
type catalytic
sequence G
description 404
source MCSA : MCSA2

16) chain B
residue 532
type catalytic
sequence V
description 404
source MCSA : MCSA2

17) chain B
residue 334
type BINDING
sequence H
description BINDING => ECO:0000250
source Swiss-Prot : SWS_FT_FI1

18) chain B
residue 479
type BINDING
sequence I
description BINDING => ECO:0000250
source Swiss-Prot : SWS_FT_FI1

19) chain B
residue 482
type BINDING
sequence G
description BINDING => ECO:0000250
source Swiss-Prot : SWS_FT_FI1

20) chain B
residue 486
type BINDING
sequence I
description BINDING => ECO:0000250
source Swiss-Prot : SWS_FT_FI1

21) chain B
residue 529
type BINDING
sequence L
description BINDING => ECO:0000250
source Swiss-Prot : SWS_FT_FI1

22) chain B
residue 282
type BINDING
sequence G
description BINDING => ECO:0000250
source Swiss-Prot : SWS_FT_FI1

23) chain B
residue 326
type BINDING
sequence A
description BINDING => ECO:0000250
source Swiss-Prot : SWS_FT_FI1

24) chain B
residue 302
type MOD_RES
sequence P
description Phosphoserine => ECO:0007744|PubMed:17330950, ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198
source Swiss-Prot : SWS_FT_FI2

25) chain B
residue 503
type MOD_RES
sequence P
description Phosphoserine => ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198
source Swiss-Prot : SWS_FT_FI3

26) chain B
residue 547
type MOD_RES
sequence L
description Phosphoserine => ECO:0007744|PubMed:17287358
source Swiss-Prot : SWS_FT_FI4


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