Structure of PDB 1mau Chain A

Receptor sequence

>1mauA (length=328) Species: 1422 (Geobacillus stearothermophilus)

MKTIFSGIQPSGVITIGNYIGALRQFVELQHEYNCYFCIVDQHAITVWQD
PHELRQNIRRLAALYLAVGIDPTQATLFIQSEVPAHAQAAWMLQCIVYIG
ELERMTQFKEKSAGKEAVSAGLLTYPPLMAADILLYNTDIVPVGEDQKQH
IELTRDLAERFNKRYGELFTIPEARIPKVGARIMSLVDPTKKMSKSDPNP
KAYITLLDDAKTIEKKIKSAVTDSEGTIRYDKEAKPGISNLLNIYSTLSG
QSIEELERQYEGKGYGVFKADLAQVVIETLRPIQERYHHWMESEELDRVL
DEGAEKANRVASEMVRKMEQAMGLGRRR

3D structure

• PDB: 1mau 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: A
• Resolution: 2.15 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	A	I8 Q9 S11 G17 N18 G21 V143 G144 D146 A181 R182 I183 K192 M193 S194 K195 S196	I8 Q9 S11 G17 N18 G21 V143 G144 D146 A181 R182 I183 K192 M193 S194 K195 S196	PDBbind-CN: -logKd/Ki=11.30,Kd=5pM
BS02	LTN	A	F5 S6 G7 H43 Y125 M129 I133 V141 Q147	F5 S6 G7 H43 Y125 M129 I133 V141 Q147

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