Logo
Information on 1evl
PDB: 1evl
Compound: threonyl-trna synthetase
Classification: LIGASE
Entry date in PDB: 2000-07-19
Resolution [Å]: 1.55
R-Factor: 0.215


CHAIN: A
SWISS-PROT/TREMBL: P00955
   KEYWORD: 3D-structure    Aminoacyl-tRNA synthetase    ATP-binding    Complete proteome    Ligase    Metal-binding    Protein biosynthesis    Repressor    RNA-binding    Translation regulation    Zinc   
EC: 6.1.1.3
SCOP: c.51.1.1 Alpha and beta proteins (a/b)    Anticodon-binding domain-like    Anticodon-binding domain of Class II aaRS    Anticodon-binding domain of Class II aaRS    Threonyl-tRNA synthetase (ThrRS), C-terminal domain    Escherichia coli
SCOP: d.104.1.1 Alpha and beta proteins (a+b)    Class II aaRS and biotin synthetases    Class II aaRS and biotin synthetases    Class II aminoacyl-tRNA synthetase (aaRS)-like, catalytic domain    Threonyl-tRNA synthetase (ThrRS)    Escherichia coli
GO:  


CHAIN: B
SWISS-PROT/TREMBL: P00955
   KEYWORD: 3D-structure    Aminoacyl-tRNA synthetase    ATP-binding    Complete proteome    Ligase    Metal-binding    Protein biosynthesis    Repressor    RNA-binding    Translation regulation    Zinc   
EC: 6.1.1.3
SCOP: c.51.1.1 Alpha and beta proteins (a/b)    Anticodon-binding domain-like    Anticodon-binding domain of Class II aaRS    Anticodon-binding domain of Class II aaRS    Threonyl-tRNA synthetase (ThrRS), C-terminal domain    Escherichia coli
SCOP: d.104.1.1 Alpha and beta proteins (a+b)    Class II aaRS and biotin synthetases    Class II aaRS and biotin synthetases    Class II aminoacyl-tRNA synthetase (aaRS)-like, catalytic domain    Threonyl-tRNA synthetase (ThrRS)    Escherichia coli
GO:  


CHAIN: C
SWISS-PROT/TREMBL: P00955
   KEYWORD: 3D-structure    Aminoacyl-tRNA synthetase    ATP-binding    Complete proteome    Ligase    Metal-binding    Protein biosynthesis    Repressor    RNA-binding    Translation regulation    Zinc   
EC: 6.1.1.3
SCOP: c.51.1.1 Alpha and beta proteins (a/b)    Anticodon-binding domain-like    Anticodon-binding domain of Class II aaRS    Anticodon-binding domain of Class II aaRS    Threonyl-tRNA synthetase (ThrRS), C-terminal domain    Escherichia coli
SCOP: d.104.1.1 Alpha and beta proteins (a+b)    Class II aaRS and biotin synthetases    Class II aaRS and biotin synthetases    Class II aminoacyl-tRNA synthetase (aaRS)-like, catalytic domain    Threonyl-tRNA synthetase (ThrRS)    Escherichia coli
GO:  


CHAIN: D
SWISS-PROT/TREMBL: P00955
   KEYWORD: 3D-structure    Aminoacyl-tRNA synthetase    ATP-binding    Complete proteome    Ligase    Metal-binding    Protein biosynthesis    Repressor    RNA-binding    Translation regulation    Zinc   
EC: 6.1.1.3
SCOP: c.51.1.1 Alpha and beta proteins (a/b)    Anticodon-binding domain-like    Anticodon-binding domain of Class II aaRS    Anticodon-binding domain of Class II aaRS    Threonyl-tRNA synthetase (ThrRS), C-terminal domain    Escherichia coli
SCOP: d.104.1.1 Alpha and beta proteins (a+b)    Class II aaRS and biotin synthetases    Class II aaRS and biotin synthetases    Class II aminoacyl-tRNA synthetase (aaRS)-like, catalytic domain    Threonyl-tRNA synthetase (ThrRS)    Escherichia coli
GO:  
1evl Image
Image Source: PDB

Stored Loops of 1evl

Loops in ArchDB-EC clusters

1evl_A_301 - HH => SUBCLASS : 1.3.12

Loops not clustered in ArchDB

1evl_A_291 - AR
1evl_A_453 - AR
1evl_A_504 - AR
1evl_A_265 - EH
1evl_A_615 - EH
1evl_A_592 - EH
1evl_A_569 - EH
1evl_A_542 - EH
1evl_A_508 - EH
1evl_A_477 - EH
1evl_A_417 - EH
1evl_A_378 - EH
1evl_A_298 - EH
1evl_A_325 - EH
1evl_A_319 - HA
1evl_A_353 - HA
1evl_A_465 - HA
1evl_A_497 - HA
1evl_A_254 - HA
1evl_A_605 - HA
1evl_A_244 - HE
1evl_A_268 - HE
1evl_A_309 - HE
1evl_A_334 - HE
1evl_A_552 - HE
1evl_A_431 - HE
1evl_A_489 - HE
1evl_A_518 - HE
1evl_A_598 - HE
1evl_A_578 - HE
1evl_A_393 - HE

Homologous structures to 1evl classified in ArchDB

1evk A - percentage of sequence identity: 100
1evk B - percentage of sequence identity: 100
1evl A - percentage of sequence identity: 100
1evl B - percentage of sequence identity: 100
1evl C - percentage of sequence identity: 100
1evl D - percentage of sequence identity: 100
1fyf A - percentage of sequence identity: 100
1fyf B - percentage of sequence identity: 100
1kog A - percentage of sequence identity: 100
1kog B - percentage of sequence identity: 100
1kog C - percentage of sequence identity: 100
1kog D - percentage of sequence identity: 100
1kog E - percentage of sequence identity: 100
1kog F - percentage of sequence identity: 100
1kog G - percentage of sequence identity: 100
1kog H - percentage of sequence identity: 100
1qf6 A - percentage of sequence identity: 100