Structure of PDB 1nj5 Chain A

Receptor sequence
>1nj5A (length=463) Species: 187420 (Methanothermobacter thermautotrophicus str. Delta H) [Search protein sequence]
EFSEWFHNILEEAEIIDQRYPVKGMHVWMPHGFMIRKNTLKILRRILDRD
HEEVLFPLLVPEDELAKEAIHVKGFEDEVYWVTHGGLSKLQRKLALRPTS
ETVMYPMFALWVRSHTDLPMRFYQVVNTFRYETKHTRPLIRVREITTFKE
AHTIHATASEAEEQVERAVEIYKEFFNSLGIPYLITRRPPWDKFPGSEYT
VAFDTLMPDGKTLQIGTVHNLGQTFARTFEIKFETPEGDHEYVHQTCYGL
SDRVIASVIAIHGDESGLCLPPDVAAHQVVIVPIIFKKAAEEVMEACREL
RSRLEAAGFRVHLDDRDIRAGRKYYEWEMRGVPLRVEIGPRDLEKGAAVI
SRRDTGEKVTADLQGIEETLRELMKDILENLRTRAWERMESEIREAETLE
EASRIVDEKRGIISFMWCGEEECGMDVEEKVRVDILGIQEEGSGTCINCG
REAPYRAYLARTY
3D structure
PDB1nj5 The structural basis of cysteine aminoacylation of tRNAPro by prolyl-tRNA synthetases
ChainA
Resolution2.8 Å
3D
structure
Catalytic site residues are labeled in the structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]
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.
Interaction with ligand
Site
#		 Ligand Ligand
chain		 Binding residues on receptor
(original residue number in PDB)		 Binding residues on receptor
(residue number reindexed from 1)		 Binding affinity
BS01 ZN A C436 C441 C464 C418 C423 C446
BS02 MG A E446 D452 E428 D434
BS03 P5A A T117 E119 R148 I158 V160 I163 F166 E168 F212 Q232 T235 H237 C265 Y266 G267 S269 R271 T99 E101 R130 I140 V142 I145 F148 E150 F194 Q214 T217 H219 C247 Y248 G249 S251 R253 PDBbind-CN: -logKd/Ki=7.30,Ki=50nM
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

View graph for
Molecular Function
View graph for
Biological Process
View graph for
Cellular Component
External links
PDB RCSB:1nj5, PDBe:1nj5, PDBj:1nj5
PDBsum1nj5
PubMed12578991
UniProtO26708|SYP_METTH Proline--tRNA ligase (Gene Name=proS)

[Back to BioLiP]