|
eF-site ID
|
1asy-ABRS |
PDB Code
|
1asy |
Chain
|
A, B, R, S |
|
click to enlarge
|
|
Title
|
CLASS II AMINOACYL TRANSFER RNA SYNTHETASES: CRYSTAL STRUCTURE OF YEAST ASPARTYL-TRNA SYNTHETASE COMPLEXED WITH TRNA ASP |
Classification
|
COMPLEX (AMINOACYL-TRNA SYNTHASE/TRNA) |
Compound
|
T-RNA (75-MER) |
Source
|
(1ASY) |
|
Sequence
|
A: |
EDTAKDNYGKLPLIQSRDSDRTGQKRVKFVDLDEAKDSDK
EVLFRARVHNTRQQGATLAFLTLRQQASLIQGLVKANKEG
TISKNMVKWAGSLNLESIVLVRGIVKKVDEPIKSATVQNL
EIHITKIYTISETPEALPILLEDASRSEAEAEAAGLPVVN
LDTRLDYRVIDLRTVTNQAIFRIQAGVCELFREYLATKKF
TEVHTPKLLGAPSEGGSSVFEVTYFKGKAYLAQSPQFNKQ
QLIVADFERVYEIGPVFRAENSNTHRHMTEFTGLDMEMAF
EEHYHEVLDTLSELFVFIFSELPKRFAHEIELVRKQYPVE
EFKLPKDGKMVRLTYKEGIEMLRAAGKEIGDFEDLSTENE
KFLGKLVRDKYDTDFYILDKFPLEIRPFYTMPDPANPKYS
NSYDFFMRGEEILSGAQRIHDHALLQERMKAHGLSPEDPG
LKDYCDGFSYGCPPHAGGGIGLERVVMFYLDLKNIRRASL
FPRDPKRLRP
|
B: |
EDTAKDNYGKLPLIQSRDSDRTGQKRVKFVDLDEAKDSDK
EVLFRARVHNTRQQGATLAFLTLRQQASLIQGLVKANKEG
TISKNMVKWAGSLNLESIVLVRGIVKKVDEPIKSATVQNL
EIHITKIYTISETPEALPILLEDASRSEAEAEAAGLPVVN
LDTRLDYRVIDLRTVTNQAIFRIQAGVCELFREYLATKKF
TEVHTPKLLGAPSEGGSSVFEVTYFKGKAYLAQSPQFNKQ
QLIVADFERVYEIGPVFRAENSNTHRHMTEFTGLDMEMAF
EEHYHEVLDTLSELFVFIFSELPKRFAHEIELVRKQYPVE
EFKLPKDGKMVRLTYKEGIEMLRAAGKEIGDFEDLSTENE
KFLGKLVRDKYDTDFYILDKFPLEIRPFYTMPDPANPKYS
NSYDFFMRGEEILSGAQRIHDHALLQERMKAHGLSPEDPG
LKDYCDGFSYGCPPHAGGGIGLERVVMFYLDLKNIRRASL
FPRDPKRLRP
|
R: |
UCCGUGAUAGUUXAAXGGXCAGAAUGGGCGCXUGUCXCGU
GCCAGAUXGGGGXXCAAUUCCCCGUCGCGGAGCCA
|
S: |
UCCGUGAUAGUUXAAXGGXCAGAAUGGGCGCXUGUCXCGU
GCCAGAUXGGGGXXCAAUUCCCCGUCGCGGAGCCA
|
|
Description
|
|
Functional site
|
|
1)
|
chain |
A |
residue |
326 |
type |
catalytic |
sequence |
A
|
description |
404
|
source |
MCSA : MCSA1
|
|
2)
|
chain |
A |
residue |
328 |
type |
catalytic |
sequence |
N
|
description |
404
|
source |
MCSA : MCSA1
|
|
3)
|
chain |
A |
residue |
334 |
type |
catalytic |
sequence |
H
|
description |
404
|
source |
MCSA : MCSA1
|
|
4)
|
chain |
A |
residue |
335 |
type |
catalytic |
sequence |
M
|
description |
404
|
source |
MCSA : MCSA1
|
|
5)
|
chain |
A |
residue |
479 |
type |
catalytic |
sequence |
I
|
description |
404
|
source |
MCSA : MCSA1
|
|
6)
|
chain |
A |
residue |
482 |
type |
catalytic |
sequence |
G
|
description |
404
|
source |
MCSA : MCSA1
|
|
7)
|
chain |
A |
residue |
532 |
type |
catalytic |
sequence |
V
|
description |
404
|
source |
MCSA : MCSA1
|
|
8)
|
chain |
B |
residue |
326 |
type |
catalytic |
sequence |
A
|
description |
404
|
source |
MCSA : MCSA2
|
|
9)
|
chain |
B |
residue |
328 |
type |
catalytic |
sequence |
N
|
description |
404
|
source |
MCSA : MCSA2
|
|
10)
|
chain |
B |
residue |
334 |
type |
catalytic |
sequence |
H
|
description |
404
|
source |
MCSA : MCSA2
|
|
11)
|
chain |
B |
residue |
335 |
type |
catalytic |
sequence |
M
|
description |
404
|
source |
MCSA : MCSA2
|
|
12)
|
chain |
B |
residue |
479 |
type |
catalytic |
sequence |
I
|
description |
404
|
source |
MCSA : MCSA2
|
|
13)
|
chain |
B |
residue |
482 |
type |
catalytic |
sequence |
G
|
description |
404
|
source |
MCSA : MCSA2
|
|
14)
|
chain |
B |
residue |
532 |
type |
catalytic |
sequence |
V
|
description |
404
|
source |
MCSA : MCSA2
|
|
15)
|
chain |
A |
residue |
282 |
type |
BINDING |
sequence |
G
|
description |
BINDING => ECO:0000250
|
source |
Swiss-Prot : SWS_FT_FI1
|
|
16)
|
chain |
B |
residue |
334 |
type |
BINDING |
sequence |
H
|
description |
BINDING => ECO:0000250
|
source |
Swiss-Prot : SWS_FT_FI1
|
|
17)
|
chain |
B |
residue |
479 |
type |
BINDING |
sequence |
I
|
description |
BINDING => ECO:0000250
|
source |
Swiss-Prot : SWS_FT_FI1
|
|
18)
|
chain |
B |
residue |
482 |
type |
BINDING |
sequence |
G
|
description |
BINDING => ECO:0000250
|
source |
Swiss-Prot : SWS_FT_FI1
|
|
19)
|
chain |
B |
residue |
486 |
type |
BINDING |
sequence |
I
|
description |
BINDING => ECO:0000250
|
source |
Swiss-Prot : SWS_FT_FI1
|
|
20)
|
chain |
B |
residue |
529 |
type |
BINDING |
sequence |
L
|
description |
BINDING => ECO:0000250
|
source |
Swiss-Prot : SWS_FT_FI1
|
|
21)
|
chain |
A |
residue |
326 |
type |
BINDING |
sequence |
A
|
description |
BINDING => ECO:0000250
|
source |
Swiss-Prot : SWS_FT_FI1
|
|
22)
|
chain |
A |
residue |
334 |
type |
BINDING |
sequence |
H
|
description |
BINDING => ECO:0000250
|
source |
Swiss-Prot : SWS_FT_FI1
|
|
23)
|
chain |
A |
residue |
479 |
type |
BINDING |
sequence |
I
|
description |
BINDING => ECO:0000250
|
source |
Swiss-Prot : SWS_FT_FI1
|
|
24)
|
chain |
A |
residue |
482 |
type |
BINDING |
sequence |
G
|
description |
BINDING => ECO:0000250
|
source |
Swiss-Prot : SWS_FT_FI1
|
|
25)
|
chain |
A |
residue |
486 |
type |
BINDING |
sequence |
I
|
description |
BINDING => ECO:0000250
|
source |
Swiss-Prot : SWS_FT_FI1
|
|
26)
|
chain |
A |
residue |
529 |
type |
BINDING |
sequence |
L
|
description |
BINDING => ECO:0000250
|
source |
Swiss-Prot : SWS_FT_FI1
|
|
27)
|
chain |
B |
residue |
282 |
type |
BINDING |
sequence |
G
|
description |
BINDING => ECO:0000250
|
source |
Swiss-Prot : SWS_FT_FI1
|
|
28)
|
chain |
B |
residue |
326 |
type |
BINDING |
sequence |
A
|
description |
BINDING => ECO:0000250
|
source |
Swiss-Prot : SWS_FT_FI1
|
|
29)
|
chain |
A |
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
|
|
30)
|
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
|
|
31)
|
chain |
A |
residue |
503 |
type |
MOD_RES |
sequence |
P
|
description |
Phosphoserine => ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198
|
source |
Swiss-Prot : SWS_FT_FI3
|
|
32)
|
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
|
|
33)
|
chain |
A |
residue |
547 |
type |
MOD_RES |
sequence |
L
|
description |
Phosphoserine => ECO:0007744|PubMed:17287358
|
source |
Swiss-Prot : SWS_FT_FI4
|
|
34)
|
chain |
B |
residue |
547 |
type |
MOD_RES |
sequence |
L
|
description |
Phosphoserine => ECO:0007744|PubMed:17287358
|
source |
Swiss-Prot : SWS_FT_FI4
|
|
|
|