Structure of PDB 2hrh Chain A Binding Site BS03

Receptor Information

>2hrh Chain A (length=496) Species: 76130 (Coriolopsis trogii)

AIGPVADLTISNGAVSPDGFSRQAILVNDVFPSPLITGNKGDRFQLNVID
NMTNHTMLKSTSIHWHGFFQHGTNWADGPAFVNQCPISTGHAFLYDFQVP
DQAGTFWYHSHLSTQYCDGLRGPIVVYDPQDPHKSLYDVDDDSTVITLAD
WYHLAAKVGSPVPTADATLINGLGRSIDTLNADLAVITVTKGKRYRFRLV
SLSCDPNHVFSIDGHSLTVIEADSVNLKPQTVDSIQIFAAQRYSFVLNAD
QDVGNYWIRALPNSGTRNFDGGVNSAILRYDGAAPVEPTTSQTPSTNPLV
ESALTTLEGTAAPGSPAPGGVDLALNMAFGFAGGKFTINGASFTPPTVPV
LLQILSGAQSAQDLLPSGSVYSLPANADIEISLPATAAAPGFPHPFHLHG
HTFAVVRSAGSSTYNYENPVYRDVVSTGSPGDNVTIRFRTDNPGPWFLHC
HIDFHLEAGFAVVMAEDIPEVAATNPVPQAWSDLCPTYDALSPDDQ

Ligand information

• Ligand ID: CU
• InChI: InChI=1S/Cu/q+2
• InChIKey: JPVYNHNXODAKFH-UHFFFAOYSA-N
• SMILES:
  ACDLabs 10.04
  OpenEye OEToolkits 1.5.0: [Cu+2]
  CACTVS 3.341: [Cu++]
• Formula: Cu
• Name: COPPER (II) ION
• DrugBank: DB14552
• PDB chain: 2hrh Chain A Residue 499

Receptor-Ligand Complex Structure

Structure summary

• PDB: 2hrh Crystal structure of the blue multicopper oxidase from the white-rot fungus Trametes trogii complexed with p-toluate
• Resolution: 2.6 Å
• Binding residue (original residue number in PDB): H111 H399 H449
• Binding residue (residue number reindexed from 1): H111 H399 H449
• Annotation score: 1

Enzymatic activity

• Catalytic site (original residue number in PDB): H64 H66 H109 H111 H394 H397 H399 H449 C450 H451 I452 H455 F460
• Catalytic site (residue number reindexed from 1): H64 H66 H109 H111 H394 H397 H399 H449 C450 H451 I452 H455 F460
• Enzyme Commision number: 1.10.3.2: laccase.

Gene Ontology

Molecular Function

• GO:0005507 copper ion binding
• GO:0016491 oxidoreductase activity
• GO:0046872 metal ion binding
• GO:0052716 hydroquinone:oxygen oxidoreductase activity

Cellular Component

• GO:0005576 extracellular region

External links

• PDB: RCSB:2hrh, PDBe:2hrh, PDBj:2hrh
• PDBsum: 2hrh
• UniProt: Q9HDQ0