Structure of PDB 5k8n Chain D Binding Site BS01

Receptor Information

>5k8n Chain D (length=420) Species: 376 (Bradyrhizobium sp.)

DVAKVMKTLDGMREGLIQTAVELGSIEAPTGREGAAGDYVYEWMARNGFG
PERVGVFDDRFNVVGRLRGTGGGASLSFNSHLDTIMAREDTARFADANDR
IYHEAWHEEGRIYGYSVVNCKGPMACWLIAAKALKEAGAALKGDVVLTAV
CGEIDCEPVDEFQGHDYLAEDIGARYAISHGAISDYALVAEATNFKPAWV
EAGKVFLKVTVFAGPSRYTPYVPRPVAALDSPNAIVRMAKLVEALEEWAD
NYEKRYTREYGGGTVVPKVAIGAIRGGVPYKIYRFPELCSIYMDIRLNPD
TNPLVVQREVEAVVSKLGLKAEVKPFLFRRGYEAQGIEPLQNALEVAHRE
VVGRPTERPGSPECSMWRDTNPYNELGIPSLTYGCGGGAGGGNTYFLVDD
MLKAAKVYAMTAMDLCNRTP

Ligand information

• Ligand ID: 6R6
• InChI: InChI=1S/C7H6N2O4/c8-6-2-1-4(9(12)13)3-5(6)7(10)11/h1-3H,8H2,(H,10,11)
• InChIKey: RUCHWTKMOWXHLU-UHFFFAOYSA-N
• SMILES:
  OpenEye OEToolkits 2.0.5: c1cc(c(cc1[N+](=O)[O-])C(=O)O)N
  CACTVS 3.385: Nc1ccc(cc1C(O)=O)[N+]([O-])=O
• Formula: C7 H6 N2 O4
• Name: 5-nitroanthranilic acid;
  2-azanyl-5-nitro-benzoic acid
• ChEMBL: CHEMBL39476
• ZINC: ZINC000003878253
• PDB chain: 5k8n Chain B Residue 501

Receptor-Ligand Complex Structure

Structure summary

• PDB: 5k8n Enzymatic hydrolysis by transition-metal-dependent nucleophilic aromatic substitution.
• Resolution: 3.225 Å
• Binding residue (original residue number in PDB): Y223 Y288
• Binding residue (residue number reindexed from 1): Y218 Y283
• Annotation score: 5

Enzymatic activity

• Enzyme Commision number: 3.5.99.8: 5-nitroanthranilic acid aminohydrolase.

Gene Ontology

Molecular Function

• GO:0016787 hydrolase activity
• GO:0046872 metal ion binding

External links

• PDB: RCSB:5k8n, PDBe:5k8n, PDBj:5k8n
• PDBsum: 5k8n
• PubMed: 27694799
• UniProt: D3WZ85|NAAA_BRASZ 5-nitroanthranilic acid aminohydrolase (Gene Name=naaA)