Structure of PDB 1m83 Chain A

Receptor sequence
>1m83A (length=328) Species: 1422 (Geobacillus stearothermophilus) [Search protein sequence]
MKTIFSGIQPSGVITIGNYIGALRQFVELQHEYNCYFCIVDQHAITVWQD
PHELRQNIRRLAALYLAVGIDPTQATLFIQSEVPAHAQAAWMLQCIVYIG
ELERMTQFKEKSAGKEAVSAGLLTYPPLMAADILLYNTDIVPVGEDQKQH
IELTRDLAERFNKRYGELFTIPEARIPKVGARIMSLVDPTKKMSKSDPNP
KAYITLLDDAKTIEKKIKSAVTDSEGTIRYDKEAKPGISNLLNIYSTLSG
QSIEELERQYEGKGYGVFKADLAQVVIETLRPIQERYHHWMESEELDRVL
DEGAEKANRVASEMVRKMEQAMGLGRRR
3D structure
PDB1m83 Interconversion of ATP binding and conformational free energies by tryptophanyl-tRNA synthetase: structures of ATP bound to open and closed, pre-transition-state conformations.
ChainA
Resolution2.2 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) K111 K192 K195
Catalytic site (residue number reindexed from 1) K111 K192 K195
Enzyme Commision number 6.1.1.2: tryptophan--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 A Q9 S11 G17 N18 G21 V143 G144 D146 A181 R182 I183 K192 M193 S194 K195 S196 Q9 S11 G17 N18 G21 V143 G144 D146 A181 R182 I183 K192 M193 S194 K195 S196 MOAD: Kd=0.4mM
PDBbind-CN: -logKd/Ki=3.40,Kd=0.4mM
Gene Ontology
Molecular Function
GO:0000166 nucleotide binding
GO:0004812 aminoacyl-tRNA ligase activity
GO:0004830 tryptophan-tRNA ligase activity
GO:0005524 ATP binding
Biological Process
GO:0006412 translation
GO:0006418 tRNA aminoacylation for protein translation
GO:0006436 tryptophanyl-tRNA aminoacylation
Cellular Component
GO:0005737 cytoplasm

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Cellular Component
External links
PDB RCSB:1m83, PDBe:1m83, PDBj:1m83
PDBsum1m83
PubMed12473451
UniProtP00953|SYW_GEOSE Tryptophan--tRNA ligase (Gene Name=trpS)

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