Structure of PDB 1b76 Chain B

Receptor sequence
>1b76B (length=442) Species: 300852 (Thermus thermophilus HB8) [Search protein sequence]
AASSLDELVALCKRRGFIFQSSEIYGGLQGVYDYGPLGVELKNNLKQAWW
RRNVYERDDMEGLDASVLTHRLVLHYSGHEATFADPMVDNAKARYWTPPR
YFNMMFQDLRGPRGGRGLLAYLRPETAQGIFVNFKNVLDATSRKLGFGIA
QIGKAFRNEITPRNFIFRVREFEQMEIEYFVRPGEDEYWHRYWVEERLKW
WQEMGLSRENLVPYQQPPESSAHYAKATVDILYRFPHGSLELEGIAQRTD
FDLGSHTKDQEALGITARVLRNEHSTQRLAYRDPETGKWFVPYVIEPSAG
VDRGVLALLAEAFTREELPNGEERIVLKLKPQLAPIKVAVIPLVKNRPEI
TEYAKRLKARLLALGLGRVLYEDTGNIGKAYRRHDEVGTPFAVTVDYDTI
GQSKDGTTRLKDTVTVRDRDTMEQIRLHVDELEGFLRERLRW
3D structure
PDB1b76 Glycyl-tRNA synthetase uses a negatively charged pit for specific recognition and activation of glycine.
ChainB
Resolution3.4 Å
3D
structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]
Enzymatic activity
Enzyme Commision number 6.1.1.14: glycine--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 ATP B R220 F230 R231 V232 F235 Q237 E304 L305 S361 G363 R366 R157 F167 R168 V169 F172 Q174 E241 L242 S298 G300 R303
Gene Ontology
Molecular Function
GO:0000166 nucleotide binding
GO:0004812 aminoacyl-tRNA ligase activity
GO:0005524 ATP binding
Biological Process
GO:0006418 tRNA aminoacylation for protein translation

View graph for
Molecular Function
View graph for
Biological Process
External links
PDB RCSB:1b76, PDBe:1b76, PDBj:1b76
PDBsum1b76
PubMed10064708
UniProtP56206|SYG_THET8 Glycine--tRNA ligase (Gene Name=glyQS)

[Back to BioLiP]