Structure of PDB 1maw Chain B

Receptor sequence

>1mawB (length=326) Species: 1422 (Geobacillus stearothermophilus)

MKTIFSGIQPSGVITIGNYIGALRQFVELQHEYNCYFCIVDQHAITVWQD
PHELRQNIRRLAALYLAVGIDPTQATLFIQSEVPAHAQAAWMLQCIVYIG
ELERMTQFKEKSAGKEAVSAGLLTYPPLMAADILLYNTDIVPVGEDQKQH
IELTRDLAERFNKRYGELFTIPEARIPKVGARIMSLVDPTKKMSKSDPNP
KAYITLLDDAKTIEKKIKSAVTDSEGTIRYDKEAKPGISNLLNIYSTLSG
QSIEELERQYEGKGYGVFKADLAQVVIETLRPIQERYHHWMESEELDRVL
DEGAEKANRVASEMVRKMEQAMGLGR

3D structure

• PDB: 1maw Interconversion of ATP binding and conformational free energies by tryptophanyl-tRNA synthetase: structures of ATP bound to open and closed, pre-transition-state conformations.
• Chain: B
• Resolution: 3.0 Å

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	B	G17 N18 G21 I183 K192 M193 S194 K195 S196	G17 N18 G21 I183 K192 M193 S194 K195 S196

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

External links

• PDB: RCSB:1maw, PDBe:1maw, PDBj:1maw
• PDBsum: 1maw
• PubMed: 12473451
• UniProt: P00953|SYW_GEOSE Tryptophan--tRNA ligase (Gene Name=trpS)