|
|
eF-site ID
|
1asy-B |
|
PDB Code
|
1asy |
|
Chain
|
B |
|
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
|
B: |
EDTAKDNYGKLPLIQSRDSDRTGQKRVKFVDLDEAKDSDK
EVLFRARVHNTRQQGATLAFLTLRQQASLIQGLVKANKEG
TISKNMVKWAGSLNLESIVLVRGIVKKVDEPIKSATVQNL
EIHITKIYTISETPEALPILLEDASRSEAEAEAAGLPVVN
LDTRLDYRVIDLRTVTNQAIFRIQAGVCELFREYLATKKF
TEVHTPKLLGAPSEGGSSVFEVTYFKGKAYLAQSPQFNKQ
QLIVADFERVYEIGPVFRAENSNTHRHMTEFTGLDMEMAF
EEHYHEVLDTLSELFVFIFSELPKRFAHEIELVRKQYPVE
EFKLPKDGKMVRLTYKEGIEMLRAAGKEIGDFEDLSTENE
KFLGKLVRDKYDTDFYILDKFPLEIRPFYTMPDPANPKYS
NSYDFFMRGEEILSGAQRIHDHALLQERMKAHGLSPEDPG
LKDYCDGFSYGCPPHAGGGIGLERVVMFYLDLKNIRRASL
FPRDPKRLRP
|
|
|
Description
|
|
Functional site
|
|
|
1)
|
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
|
|
|
2)
|
chain |
B |
| residue |
326 |
| type |
catalytic |
| sequence |
A
|
| description |
404
|
| source |
MCSA : MCSA2
|
|
|
3)
|
chain |
B |
| residue |
328 |
| type |
catalytic |
| sequence |
N
|
| description |
404
|
| source |
MCSA : MCSA2
|
|
|
4)
|
chain |
B |
| residue |
334 |
| type |
catalytic |
| sequence |
H
|
| description |
404
|
| source |
MCSA : MCSA2
|
|
|
5)
|
chain |
B |
| residue |
335 |
| type |
catalytic |
| sequence |
M
|
| description |
404
|
| source |
MCSA : MCSA2
|
|
|
6)
|
chain |
B |
| residue |
479 |
| type |
catalytic |
| sequence |
I
|
| description |
404
|
| source |
MCSA : MCSA2
|
|
|
7)
|
chain |
B |
| residue |
482 |
| type |
catalytic |
| sequence |
G
|
| description |
404
|
| source |
MCSA : MCSA2
|
|
|
8)
|
chain |
B |
| residue |
532 |
| type |
catalytic |
| sequence |
V
|
| description |
404
|
| source |
MCSA : MCSA2
|
|
|
9)
|
chain |
B |
| residue |
547 |
| type |
MOD_RES |
| sequence |
L
|
| description |
Phosphoserine => ECO:0007744|PubMed:17287358
|
| source |
Swiss-Prot : SWS_FT_FI4
|
|
|
10)
|
chain |
B |
| residue |
334 |
| type |
BINDING |
| sequence |
H
|
| description |
BINDING => ECO:0000250
|
| source |
Swiss-Prot : SWS_FT_FI1
|
|
|
11)
|
chain |
B |
| residue |
479 |
| type |
BINDING |
| sequence |
I
|
| description |
BINDING => ECO:0000250
|
| source |
Swiss-Prot : SWS_FT_FI1
|
|
|
12)
|
chain |
B |
| residue |
482 |
| type |
BINDING |
| sequence |
G
|
| description |
BINDING => ECO:0000250
|
| source |
Swiss-Prot : SWS_FT_FI1
|
|
|
13)
|
chain |
B |
| residue |
486 |
| type |
BINDING |
| sequence |
I
|
| description |
BINDING => ECO:0000250
|
| source |
Swiss-Prot : SWS_FT_FI1
|
|
|
14)
|
chain |
B |
| residue |
529 |
| type |
BINDING |
| sequence |
L
|
| description |
BINDING => ECO:0000250
|
| source |
Swiss-Prot : SWS_FT_FI1
|
|
|
15)
|
chain |
B |
| residue |
282 |
| type |
BINDING |
| sequence |
G
|
| description |
BINDING => ECO:0000250
|
| source |
Swiss-Prot : SWS_FT_FI1
|
|
|
16)
|
chain |
B |
| residue |
326 |
| type |
BINDING |
| sequence |
A
|
| description |
BINDING => ECO:0000250
|
| source |
Swiss-Prot : SWS_FT_FI1
|
|
|
17)
|
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
|
|
|
|