Structure of PDB 1ses Chain A

Receptor sequence

>1sesA (length=421) Species: 274 (Thermus thermophilus)

MVDLKRLRQEPEVFHRAIREKGVALDLEALLALDREVQELKKRLQEVQTE
RNQVAKRVPKAPPEEKEALIARGKALGEEAKRLEEALREKEARLEALLLQ
VPLPPWPGAPVGGEEANREIKRVGGPPEFSFPPLDHVALMEKNGWWEPRI
SQVSGSRSYALKGDLALYELALLRFAMDFMARRGFLPMTLPSYAREKAFL
GTGHFPAYRDQVWAIAETDLYLTGTAEVVLNALHSGEILPYEALPLRYAG
YAPAFRSEAGSFGKDVRGLMRVHQFHKVEQYVLTEASLEASDRAFQELLE
NAEEILRLLELPYRLVEVATGDMGPGKWRQVDIEVYLPSEGRYRETHSCS
ALLDWQARRANLRYRDPEGRVRYAYTLNNTALATPRILAMLLENHQLQDG
RVRVPQALIPYMGKEVLEPCG

3D structure

• PDB: 1ses Crystal structures at 2.5 angstrom resolution of seryl-tRNA synthetase complexed with two analogs of seryl adenylate.
• Chain: A
• Resolution: 2.5 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): R256 R271 E345 S348 R386
• Catalytic site (residue number reindexed from 1): R256 R271 E345 S348 R386
• Enzyme Commision number: 6.1.1.11: serine--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	AHX	A	T225 R256 E258 V272 F275 K277 E279 E345 T346 S348 N378 T380 A383 R386	T225 R256 E258 V272 F275 K277 E279 E345 T346 S348 N378 T380 A383 R386

Gene Ontology

Molecular Function

• GO:0000049 tRNA binding
• GO:0000166 nucleotide binding
• GO:0004812 aminoacyl-tRNA ligase activity
• GO:0004828 serine-tRNA ligase activity
• GO:0005524 ATP binding
• GO:0042802 identical protein binding
• GO:0042803 protein homodimerization activity
• GO:0070905 serine binding

Biological Process

• GO:0006412 translation
• GO:0006418 tRNA aminoacylation for protein translation
• GO:0006434 seryl-tRNA aminoacylation
• GO:0016260 selenocysteine biosynthetic process

Cellular Component

• GO:0005737 cytoplasm

External links

• PDB: RCSB:1ses, PDBe:1ses, PDBj:1ses
• PDBsum: 1ses
• PubMed: 8128224
• UniProt: P34945|SYS_THET2 Serine--tRNA ligase (Gene Name=serS)