Structure of PDB 1kog Chain G

Receptor sequence

>1kogG (length=401) Species: 562 (Escherichia coli)

RDHRKIGKQLDLYHMQEEAPGMVFWHNDGWTIFRELEVFVRSKLKEYQYQ
EVKGPFMMDRVLWEKTGHWDNYKDAMFTTSSENREYCIKPMNCPGHVQIF
NQGLKSYRDLPLRMAEFGSCHRNEPSGSLHGLMRVRGFTQDDAHIFCTEE
QIRDEVNGCIRLVYDMYSTFGFEKIVVKLSTRPEKRIGSDEMWDRAEADL
AVALEENNIPFEYQLGEGAFYGPKIEFTLYDCLDRAWQCGTVQLDFSLPS
RLSASYVGEDNERKVPVMIHRAILGSMERFIGILTEEFAGFFPTWLAPVQ
VVIMNITDSQSEYVNELTQKLSNAGIRVKADLRNEKIGFKIREHTLRRVP
YMLVCGDKEVESGKVAVRTRRGKDLGSMDVNEVIEKLQQEIRSRSLKQLE
E

3D structure

• PDB: 1kog Structural basis of translational control by Escherichia coli threonyl tRNA synthetase.
• Chain: G
• Resolution: 3.5 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): Q381 D383 K465
• Catalytic site (residue number reindexed from 1): Q140 D142 K224
• Enzyme Commision number: 6.1.1.3: threonine--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	rna	G	K246 K249 I547 T548 D549 N575 K577 F580 I582 R583 T586 G597 K599 E600 A607 R609	K5 K8 I306 T307 D308 N334 K336 F339 I341 R342 T345 G356 K358 E359 A366 R368	PDBbind-CN: Kd=0.01uM
BS02	ZN	G	C334 H385 H511	C93 H144 H270
BS03	TSB	G	M332 R363 E365 V376 F379 Q381 D383 H385 Q479 C480 T482 Q484 H511 R512 G516 S517 R520	M91 R122 E124 V135 F138 Q140 D142 H144 Q238 C239 T241 Q243 H270 R271 G275 S276 R279

Gene Ontology

Molecular Function

• GO:0000166 nucleotide binding
• GO:0004812 aminoacyl-tRNA ligase activity
• GO:0004829 threonine-tRNA ligase activity
• GO:0005524 ATP binding

Biological Process

• GO:0006418 tRNA aminoacylation for protein translation
• GO:0006435 threonyl-tRNA aminoacylation

Cellular Component

• GO:0005737 cytoplasm

External links

• PDB: RCSB:1kog, PDBe:1kog, PDBj:1kog
• PDBsum: 1kog
• PubMed: 11953757
• UniProt: P0A8M3|SYT_ECOLI Threonine--tRNA ligase (Gene Name=thrS)