Structure of PDB 4a2f Chain A

Receptor sequence

>4a2fA (length=496) Species: 76126 (Coriolopsis gallica)

AIGPVADLTISNGAVSPDGFSRQAILVNDVFPSPLITGNKGDRFQLNVID
NMTNHTMLKSTSIHWHGFFQHGTNWADGPAFVNQCPISTGHAFLYDFQVP
DQAGTFWYHSHLSTQYCDGLRGPIVVYDPNDPHASLYDVDDDSTVITLAD
WYHLAAKVGAPVPTADATLINGLGRSAATLAADLAVITVTKGKRYRFRLV
SLSCDPNYTFSIDGHSLTVIEADSVNLKPHTVDSLQIFAAQRYSFVLNAD
QDVDNYWIRALPNSGTQNFAGGTNSAILRYDGAAPVEPTTSQTPSTNPLV
ESALTTLKGTAAPGSPTPGGVDLALNMAFGFAGGNFTINGASFTPPTVPV
LLQILSGAQSAADLLPAGSVYSLPANADIEISLPATAAAPGFPHPFHLHG
HVFAVVRSAGSSTYNYANPVYRDVVSTGAPGDNVTIRFRTDNPGPWFLHC
HIDFHLEAGFAVVMAEDIPDVAATNPVPQAWSDLCPTYDALSPDDQ

3D structure

• PDB: 4a2f Structural Changes Caused by Radiation-Induced Reduction and Radiolysis: The Effect of X-Ray Absorbed Dose in a Fungal Multicopper Oxidase
• Chain: A
• Resolution: 1.9 Å

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.

Interaction with ligand

Site #	Ligand	Ligand chain	Binding residues on receptor (original residue number in PDB)	Binding residues on receptor (residue number reindexed from 1)	Binding affinity
BS01	CU	A	H415 C471 H476	H394 C450 H455
BS02	CU	A	H87 H130 H472	H66 H109 H451
BS03	CU	A	H132 H420 H470	H111 H399 H449

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:4a2f, PDBe:4a2f, PDBj:4a2f
• PDBsum: 4a2f
• PubMed: 22525754
• UniProt: Q1W6B1