Structure of PDB 4o2d Chain B Binding Site BS01

Receptor Information
>4o2d Chain B (length=515) Species: 246196 (Mycolicibacterium smegmatis MC2 155) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
VLRTHAAGSLRPADAGQTVTLAGWVARRRDHGGVIFIDLRDASGVSQVVF
REGDVLAAAHRLRAEFCVAVTGVVEVRPEGNENPEIPTGQIEVNATELTV
LGESAPLPFQLDEQAGEEARLKYRYLDLRREGPGNALRLRSKVNAAARSV
LAEHDFVEIETPTLTRSTPEGARDFLVPARLQPGSFYALPQSPQLFKQLL
MVAGMERYYQIARCYRDEDFDRQPEFTQLDMEMSFVEADDVIAISEQVLK
AVWATIGYDLPLPLPRISYEEAMRRFGSDKPDLRFGIELVECTEYFPYVG
AVVMPWQEFAKQRGFFAAGPAKGARALLGATRIEIAKRLDLIDPNAWAFT
WVVDFPMFEAADEATAAGDVAVGSGAWTAMHHAFTAPKPDSVDTFDSDPG
NALSDAYDIVCNGNEIGGGSIRIHRRDIQERVFAMMGIDHDEAQEKFGFL
LDAFSYGAPPHGGIAFGWDRITALLAGVDSIREVIAFPKSGGGVDPLTDA
PAPITPQQRKESGID
Ligand information
Ligand IDASP
InChIInChI=1S/C4H7NO4/c5-2(4(8)9)1-3(6)7/h2H,1,5H2,(H,6,7)(H,8,9)/t2-/m0/s1
InChIKeyCKLJMWTZIZZHCS-REOHCLBHSA-N
SMILES
SoftwareSMILES
OpenEye OEToolkits 1.7.0C(C(C(=O)O)N)C(=O)O
OpenEye OEToolkits 1.7.0C([C@@H](C(=O)O)N)C(=O)O
CACTVS 3.370N[CH](CC(O)=O)C(O)=O
CACTVS 3.370N[C@@H](CC(O)=O)C(O)=O
ACDLabs 12.01O=C(O)CC(N)C(=O)O
FormulaC4 H7 N O4
NameASPARTIC ACID
ChEMBLCHEMBL274323
DrugBankDB00128
ZINCZINC000000895032
PDB chain4o2d Chain B Residue 801 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
Global viewLocal viewStructure summary

[Spin on] [Spin off] [Reset]
[High quality] [Low quality]
[White background] [Black background]
[Spin on] [Spin off] [Reset]
[High quality] [Low quality]
[White background] [Black background]
PDB4o2d Increasing the structural coverage of tuberculosis drug targets.
Resolution2.6 Å
Binding residue
(original residue number in PDB)		E171 S193 Q195 Q231 H450 G486 R490 I532 A533
Binding residue
(residue number reindexed from 1)		E170 S192 Q194 Q228 H382 G418 R422 I464 A465
Annotation score5
Enzymatic activity
Catalytic site (original residue number in PDB) R217 E219 R225 Q226 E483 G486 R538
Catalytic site (residue number reindexed from 1) R216 E218 R222 Q223 E415 G418 R470
Enzyme Commision number 6.1.1.23: aspartate--tRNA(Asn) ligase.
Gene Ontology
Molecular Function
GO:0000166 nucleotide binding
GO:0003676 nucleic acid binding
GO:0004812 aminoacyl-tRNA ligase activity
GO:0004815 aspartate-tRNA ligase activity
GO:0005524 ATP binding
GO:0016874 ligase activity
GO:0050560 aspartate-tRNA(Asn) ligase activity
Biological Process
GO:0006412 translation
GO:0006418 tRNA aminoacylation for protein translation
GO:0006422 aspartyl-tRNA aminoacylation
Cellular Component
GO:0005737 cytoplasm

View graph for
Molecular Function
View graph for
Biological Process
View graph for
Cellular Component
External links
PDB RCSB:4o2d, PDBe:4o2d, PDBj:4o2d
PDBsum4o2d
PubMed25613812
UniProtA0QWN3|SYDND_MYCS2 Aspartate--tRNA(Asp/Asn) ligase (Gene Name=aspS)

[Back to BioLiP]