Structure of PDB 1ggm Chain B

Receptor sequence
>1ggmB (length=442) Species: 300852 (Thermus thermophilus HB8) [Search protein sequence]
AASSLDELVALCKRRGFIFQSSEIYGGLQGVYDYGPLGVELKNNLKQAWW
RRNVYERDDMEGLDASVLTHRLVLHYSGHEATFADPMVDNAKARYWTPPR
YFNMMFQDLRGPRGGRGLLAYLRPETAQGIFVNFKNVLDATSRKLGFGIA
QIGKAFRNEITPRNFIFRVREFEQMEIEYFVRPGEDEYWHRYWVEERLKW
WQEMGLSRENLVPYQQPPESSAHYAKATVDILYRFPHGSLELEGIAQRTD
FDLGSHTKDQEALGITARVLRNEHSTQRLAYRDPETGKWFVPYVIEPSAG
VDRGVLALLAEAFTREELPNGEERIVLKLKPQLAPIKVAVIPLVKNRPEI
TEYAKRLKARLLALGLGRVLYEDTGNIGKAYRRHDEVGTPFAVTVDYDTI
GQSKDGTTRLKDTVTVRDRDTMEQIRLHVDELEGFLRERLRW
3D structure
PDB1ggm Glycyl-tRNA synthetase uses a negatively charged pit for specific recognition and activation of glycine.
ChainB
Resolution3.4 Å
3D
structure
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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 GAP B E188 R220 F230 V232 F235 Q237 E239 E304 L305 E306 R311 E359 S361 G363 E125 R157 F167 V169 F172 Q174 E176 E241 L242 E243 R248 E296 S298 G300
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

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Molecular Function

View graph for
Biological Process
External links
PDB RCSB:1ggm, PDBe:1ggm, PDBj:1ggm
PDBsum1ggm
PubMed10064708
UniProtP56206|SYG_THET8 Glycine--tRNA ligase (Gene Name=glyQS)

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