Structure of PDB 4a2h Chain A

Receptor sequence

>4a2hA (length=495) Species: 76126 (Coriolopsis gallica)

AIGPVADLTISNGAVSPDGFSRQAILVNDVFPSPLITGNKGDRFQLNVID
NMTNHTMLKSTSIHWHGFFQHGTNWADGPAFVNQCPISTGHAFLYDFQVP
DQAGTFWYHSHLSTQYCDGLRGPIVVYDPNDPHASLYDVDDDSTVITLAD
WYHLAAKVGAPVPTADATLINGLGRSAATLAADLAVITVTKGKRYRFRLV
SLSCDPNYTFSIDGHSLTVIEADSVNLKPHTVDSLQIFAAQRYSFVLNAD
QDVDNYWIRALPNSGTQNFAGGTNSAILRYGAAPVEPTTSQTPSTNPLVE
SALTTLKGTAAPGSPTPGGVDLALNMAFGFAGGNFTINGASFTPPTVPVL
LQILSGAQSAADLLPAGSVYSLPANADIEISLPATAAAPGFPHPFHLHGH
VFAVVRSAGSSTYNYANPVYRDVVSTGAPGDNVTIRFRTDNPGPWFLHCH
IDFHLEAGFAVVMAEDIPDVAATNPVPQAWSDLCPTYDALSPDDQ

3D structure

• PDB: 4a2h Structural Changes Caused by Radiation-Induced Reduction and Radiolysis: The Effect of X-Ray Absorbed Dose in a Fungal Multicopper Oxidase
• Chain: A
• Resolution: 2.3 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 H393 H396 H398 H448 C449 H450 I451 H454 F459
• 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	H393 C449 H454
BS02	CU	A	H132 H420 H470	H111 H398 H448
BS03	CU	A	H87 H130 H472	H66 H109 H450
BS04	CU	A	H85 H87 H418	H64 H66 H396

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:4a2h, PDBe:4a2h, PDBj:4a2h
• PDBsum: 4a2h
• PubMed: 22525754
• UniProt: Q1W6B1