Structure of PDB 1ati Chain B Binding Site BS01

Receptor Information
>1ati Chain B (length=436) Species: 300852 (Thermus thermophilus HB8) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
AASSLDELVALCKRRGFIFQSSEIYGGLQGVYDYGPLGVELKNNLKQAWW
RRNVYERDDMEGLDASVLTHRLVLHYSGHEATFADPMVDWTPPRYFNMMF
QDLRGPRGGRGLLAYLRPETAQGIFVNFKNVLDATSRKLGFGIAQIGKAF
RNEITPRNFIFRVREFEQMEIEYFVRPGEDEYWHRYWVEERLKWWQEMGL
SRENLVPYQQPPESSAHYAKATVDILYRFPHGSLELEGIAQRTDFDLGSH
TKDQEALGITARVLRNEHSTQRLAYRDPETGKWFVPYVIEPSAGVDRGVL
ALLAEAFTREELPNGEERIVLKLKPQLAPIKVAVIPLVKNRPEITEYAKR
LKARLLALGLGRVLYEDTGNIGKAYRRHDEVGTPFAVTVDYDTIGQSKDG
TTRLKDTVTVRDRDTMEQIRLHVDELEGFLRERLRW
Ligand information
>1ati Chain D (length=16) Species: 300852 (Thermus thermophilus HB8) [Search peptide sequence] [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
AAAAAAAAAAGGAAAA
Receptor-Ligand Complex Structure
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PDB1ati Crystal structure of glycyl-tRNA synthetase from Thermus thermophilus.
Resolution2.75 Å
Binding residue
(original residue number in PDB)		P161 P162
Binding residue
(residue number reindexed from 1)		P92 P93
Enzymatic activity
Enzyme Commision number 6.1.1.14: glycine--tRNA ligase.
Gene Ontology
Molecular Function
GO:0000166 nucleotide binding
GO:0000287 magnesium ion binding
GO:0004812 aminoacyl-tRNA ligase activity
GO:0004820 glycine-tRNA ligase activity
GO:0005524 ATP binding
GO:0016594 glycine binding
GO:0042802 identical protein binding
GO:0046983 protein dimerization activity
Biological Process
GO:0006412 translation
GO:0006418 tRNA aminoacylation for protein translation
GO:0006426 glycyl-tRNA aminoacylation
Cellular Component
GO:0005737 cytoplasm
GO:0009345 glycine-tRNA ligase complex

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:1ati, PDBe:1ati, PDBj:1ati
PDBsum1ati
PubMed7556056
UniProtP56206|SYG_THET8 Glycine--tRNA ligase (Gene Name=glyQS)

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