1TYB

STRUCTURAL ANALYSIS OF A SERIES OF MUTANTS OF TYROSYL-TRNA SYNTHETASE: ENHANCEMENT OF CATALYSIS BY HYDROPHOBIC INTERACTIONS

Functional Information from GO Data

Chain	GOid	namespace	contents
E	0000166	molecular_function	nucleotide binding
E	0004812	molecular_function	aminoacyl-tRNA ligase activity
E	0004831	molecular_function	tyrosine-tRNA ligase activity
E	0005524	molecular_function	ATP binding
E	0006418	biological_process	tRNA aminoacylation for protein translation
E	0006437	biological_process	tyrosyl-tRNA aminoacylation

Functional Information from PDB Data

site_id	AC1
Number of Residues	11
Details	BINDING SITE FOR RESIDUE TYR E 320

Functional Information from PROSITE/UniProt

site_id	PS00178
Number of Residues	11
Details	AA_TRNA_LIGASE_I Aminoacyl-transfer RNA synthetases class-I signature. Pt.ADsLHIGHL

Chain	Residue	Details
E	PRO39-LEU49

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	9
Details	Motif: {"description":"'HIGH' region","evidences":[{"source":"PubMed","id":"11023794","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	4
Details	Motif: {"description":"'KMSKS' region","evidences":[{"source":"PubMed","id":"10630994","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	2
Details	Binding site: {"evidences":[{"source":"PDB","id":"1TYD","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI4
Number of Residues	2
Details	Binding site: {"evidences":[{"evidenceCode":"ECO:0000250"},{"source":"PDB","id":"1TYD","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI5
Number of Residues	1
Details	Binding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

Catalytic Information from CSA

site_id	CSA1
Number of Residues	2
Details	Annotated By Reference To The Literature 1d2r

site_id	CSA2
Number of Residues	4
Details	Annotated By Reference To The Literature 1d2r

Chain

Residue

Details