Structure of PDB 1nj1 Chain A Binding Site BS02

Receptor Information
>1nj1 Chain A (length=463) Species: 145262 (Methanothermobacter thermautotrophicus) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
EFSEWFHNILEEAEIIDQRYPVKGMHVWMPHGFMIRKNTLKILRRILDRD
HEEVLFPLLVPEDELAKEAIHVKGFEDEVYWVTHGGLSKLQRKLALRPTS
ETVMYPMFALWVRSHTDLPMRFYQVVNTFRYETKHTRPLIRVREITTFKE
AHTIHATASEAEEQVERAVEIYKEFFNSLGIPYLITRRPPWDKFPGSEYT
VAFDTLMPDGKTLQIGTVHNLGQTFARTFEIKFETPEGDHEYVHQTCYGL
SDRVIASVIAIHGDESGLCLPPDVAAHQVVIVPIIFKKAAEEVMEACREL
RSRLEAAGFRVHLDDRDIRAGRKYYEWEMRGVPLRVEIGPRDLEKGAAVI
SRRDTGEKVTADLQGIEETLRELMKDILENLRTRAWERMESEIREAETLE
EASRIVDEKRGIISFMWCGEEECGMDVEEKVRVDILGIQEEGSGTCINCG
REAPYRAYLARTY
Ligand information
Ligand IDMG
InChIInChI=1S/Mg/q+2
InChIKeyJLVVSXFLKOJNIY-UHFFFAOYSA-N
SMILES
SoftwareSMILES
ACDLabs 10.04
OpenEye OEToolkits 1.5.0		[Mg+2]
CACTVS 3.341[Mg++]
FormulaMg
NameMAGNESIUM ION
ChEMBL
DrugBankDB01378
ZINC
PDB chain1nj1 Chain A Residue 514 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB1nj1 The structural basis of cysteine aminoacylation of tRNAPro by prolyl-tRNA synthetases
Resolution2.55 Å
Binding residue
(original residue number in PDB)		D210 E446 D452
Binding residue
(residue number reindexed from 1)		D192 E428 D434
Annotation score1
Enzymatic activity
Catalytic site (original residue number in PDB) E119 R148 H170
Catalytic site (residue number reindexed from 1) E101 R130 H152
Enzyme Commision number 6.1.1.15: proline--tRNA ligase.
Gene Ontology
Molecular Function
GO:0000166 nucleotide binding
GO:0004812 aminoacyl-tRNA ligase activity
GO:0004827 proline-tRNA ligase activity
GO:0005515 protein binding
GO:0005524 ATP binding
GO:0046872 metal ion binding
Biological Process
GO:0006412 translation
GO:0006418 tRNA aminoacylation for protein translation
GO:0006433 prolyl-tRNA aminoacylation
Cellular Component
GO:0005737 cytoplasm
GO:0017101 aminoacyl-tRNA synthetase multienzyme complex

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:1nj1, PDBe:1nj1, PDBj:1nj1
PDBsum1nj1
PubMed12578991
UniProtO26708|SYP_METTH Proline--tRNA ligase (Gene Name=proS)

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