Structure of PDB 4ghh Chain D Binding Site BS02

Receptor Information

>4ghh Chain D (length=359) Species: 47914 (Brevibacterium fuscum)

EIPKPVAPAPDILRCAYAELVVTDLAKSRNFYVDVLGLHVSYEDENQIYL
RSFEEFIHHNLVLTKGPVAALKAMAFRVRTPEDVDKAEAYYQELGCRTER
RKDGFVKGIGDALRVEDPLGFPYEFFFETTHVERLHMRYDLYSAGELVRL
DHFNQVTPDVPRGRKYLEDLGFRVTEDIQDDEGTTYAAWMHRKGTVHDTA
LTGGNGPRLHHVAFSTHEKHNIIQICDKMGALRISDRIERGPGRHGVSNA
FYLYILDPDNHRIEIYTQDYYTGDPDNPTITWNVHDNQRRDWWGNPVVPS
WYTEASKVLDLDGNVQEIIERTDDSELEVTIGADGFSFTRAGDEDGSYHG
QASKGFKLG

Ligand information

• Ligand ID: 4NC
• InChI: InChI=1S/C6H5NO4/c8-5-2-1-4(7(10)11)3-6(5)9/h1-3,8-9H
• InChIKey: XJNPNXSISMKQEX-UHFFFAOYSA-N
• SMILES:
  CACTVS 3.341: Oc1ccc(cc1O)[N+]([O-])=O
  ACDLabs 10.04: [O-][N+](=O)c1cc(O)c(O)cc1
  OpenEye OEToolkits 1.5.0: c1cc(c(cc1[N+](=O)[O-])O)O
• Formula: C6 H5 N O4
• Name: 4-NITROCATECHOL
• ChEMBL: CHEMBL42423
• DrugBank: DB03407
• ZINC: ZINC000034800312
• PDB chain: 4ghh Chain D Residue 403

Receptor-Ligand Complex Structure

Structure summary

• PDB: 4ghh Structural basis for the role of tyrosine 257 of homoprotocatechuate 2,3-dioxygenase in substrate and oxygen activation.
• Resolution: 1.55 Å
• Binding residue (original residue number in PDB): H155 W192 H200 H214 H248 V250 Y257 E267 R293
• Binding residue (residue number reindexed from 1): H152 W189 H197 H211 H245 V247 Y254 E264 R290
• Annotation score: 1

Enzymatic activity

• Catalytic site (original residue number in PDB): H155 H200 H214 H248 Y257 E267
• Catalytic site (residue number reindexed from 1): H152 H197 H211 H245 Y254 E264
• Enzyme Commision number: 1.13.11.15: 3,4-dihydroxyphenylacetate 2,3-dioxygenase.

Gene Ontology

Molecular Function

• GO:0046872 metal ion binding
• GO:0051213 dioxygenase activity

External links

• PDB: RCSB:4ghh, PDBe:4ghh, PDBj:4ghh
• PDBsum: 4ghh
• PubMed: 23066739
• UniProt: Q45135