Structure of PDB 2ct8 Chain A

Receptor sequence

>2ct8A (length=465) Species: 63363 (Aquifex aeolicus)

MTLMKKFYVTTPIYYVNDVPHLGHAYTTIAADTIARYYRLRDYDVFFLTG
TDEHGLKIQKKAEELGISPKELVDRNAERFKKLWEFLKIEYTKFIRTTDP
YHVKFVQKVFEECYKRGDIYLGEYEKEPSYFFRLSKYQDKLLELYEKNPE
FIQPDYRRNEIISFVKQGLKDLSVTRPRSRVKWGIPVPFDPEHTIYVWFD
ALFNYISALEDKVEIYWPADLHLVGKDILRFHTVYWPAFLMSLGYELPKK
VFAHGWWTVEGKKMSKTLGNVVDPYEVVQEYGLDEVRYFLLREVPFGQDG
DFSKKAILNRINGELANEIGNLYSRVVNMAHKFLGGEVSGARDEEYAKIA
QESIKNYENYMEKVNFYKAIEEILKFTSYLNKYVDEKQPWALNKERKKEE
LQKVLYALVDGLFVLTHLLYPITPNKMKEALQMLGEKEFLKELKPYSKNT
YKLGERKILFPKREG

3D structure

• PDB: 2ct8 Structural basis for anticodon recognition by methionyl-tRNA synthetase.
• Chain: A
• Resolution: 2.7 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): I13 W230 I260 K295 K298
• Catalytic site (residue number reindexed from 1): I13 W198 I228 K263 K266
• Enzyme Commision number: 6.1.1.10: methionine--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	A	R189 E192 N349 G352 N353 S356 R357 N360 M361 N413 D417 W422 R488 I490 F492 K494	R157 E160 N317 G320 N321 S324 R325 N328 M329 N381 D385 W390 R456 I458 F460 K462
BS02	MSP	A	P12 I13 Y14 Y15 H21 G23 H24 D52 W230 A233 Y237 G257 D259 I260 H264 H286 W288 W289	P12 I13 Y14 Y15 H21 G23 H24 D52 W198 A201 Y205 G225 D227 I228 H232 H254 W256 W257

Gene Ontology

Molecular Function

• GO:0000166 nucleotide binding
• GO:0004812 aminoacyl-tRNA ligase activity
• GO:0004825 methionine-tRNA ligase activity
• GO:0005524 ATP binding
• GO:0046872 metal ion binding

Biological Process

• GO:0006412 translation
• GO:0006418 tRNA aminoacylation for protein translation
• GO:0006431 methionyl-tRNA aminoacylation

Cellular Component

• GO:0005737 cytoplasm

External links

• PDB: RCSB:2ct8, PDBe:2ct8, PDBj:2ct8
• PDBsum: 2ct8
• PubMed: 16155581
• UniProt: O67298|SYM_AQUAE Methionine--tRNA ligase (Gene Name=metG)