Structure of PDB 4a2e Chain A Binding Site BS04

Receptor Information

>4a2e Chain A (length=496) Species: 76126 (Coriolopsis gallica)

AIGPVADLTISNGAVSPDGFSRQAILVNDVFPSPLITGNKGDRFQLNVID
NMTNHTMLKSTSIHWHGFFQHGTNWADGPAFVNQCPISTGHAFLYDFQVP
DQAGTFWYHSHLSTQYCDGLRGPIVVYDPNDPHASLYDVDDDSTVITLAD
WYHLAAKVGAPVPTADATLINGLGRSAATLAADLAVITVTKGKRYRFRLV
SLSCDPNYTFSIDGHSLTVIEADSVNLKPHTVDSLQIFAAQRYSFVLNAD
QDVDNYWIRALPNSGTQNFAGGTNSAILRYDGAAPVEPTTSQTPSTNPLV
ESALTTLKGTAAPGSPTPGGVDLALNMAFGFAGGNFTINGASFTPPTVPV
LLQILSGAQSAADLLPAGSVYSLPANADIEISLPATAAAPGFPHPFHLHG
HVFAVVRSAGSSTYNYANPVYRDVVSTGAPGDNVTIRFRTDNPGPWFLHC
HIDFHLEAGFAVVMAEDIPDVAATNPVPQAWSDLCPTYDALSPDDQ

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: 4a2e Chain A Residue 1521

Receptor-Ligand Complex Structure

Structure summary

• PDB: 4a2e Structural Changes Caused by Radiation-Induced Reduction and Radiolysis: The Effect of X-Ray Absorbed Dose in a Fungal Multicopper Oxidase
• Resolution: 1.8 Å
• Binding residue (original residue number in PDB): H415 C471 H476
• Binding residue (residue number reindexed from 1): H394 C450 H455
• Annotation score: 1

Enzymatic activity

• Catalytic site (original residue number in PDB): H85 H87 H130 H132 H415 H418 H420 H470 C471 H472 I473 H476 F481
• 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:4a2e, PDBe:4a2e, PDBj:4a2e
• PDBsum: 4a2e
• PubMed: 22525754
• UniProt: Q1W6B1