Structure of PDB 1a65 Chain A

Receptor sequence

>1a65A (length=504) Species: 5346 (Coprinopsis cinerea)

QIVNSVDTMTLTNANVSPDGFTRAGILVNGVHGPLIRGGKNDNFELNVVN
DLDNPTMLRPTSIHWHGLFQRGTNWADGADGVNQCPISPGHAFLYKFTPA
GHAGTFWYHSHFGTQYCDGLRGPMVIYDDNDPHAALYDEDDENTIITLAD
WYHIPAPSIQGAAQPDATLINGKGRYVGGPAAELSIVNVEQGKKYRMRLI
SLSCDPNWQFSIDGHELTIIEVDGELTEPHTVDRLQIFTGQRYSFVLDAN
QPVDNYWIRAQPNKGRNGLAGTFANGVNSAILRYAGAANADPTTSANPNP
AQLNEADLHALIDPAAPGIPTPGAADVNLRFQLGFSGGRFTINGTAYESP
SVPTLLQIMSGAQSANDLLPAGSVYELPRNQVVELVVPAGVLGGPHPFHL
HGHAFSVVRSAGSSTYNFVNPVKRDVVSLGVTGDEVTIRFVTDNPGPWFF
HCHIEFHLMNGLAIVFAEDMANTVDANNPPVEWAQLCEIYDDLPPEATSI
QTVV

3D structure

• PDB: 1a65 Crystal structure of the type-2 Cu depleted laccase from Coprinus cinereus at 2.2 A resolution.
• Chain: A
• Resolution: 2.23 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): H64 H66 H109 H111 H396 H399 H401 H451 C452 H453 I454 H457 L462
• Catalytic site (residue number reindexed from 1): H64 H66 H109 H111 H396 H399 H401 H451 C452 H453 I454 H457 L462
• 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	H396 C452 H457	H396 C452 H457
BS02	CU	A	H111 H399 H401 H451	H111 H399 H401 H451
BS03	CU	A	H66 H109 H453	H66 H109 H453
BS04	O	A	H109 H111 H399 H451 H453	H109 H111 H399 H451 H453

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:1a65, PDBe:1a65, PDBj:1a65
• PDBsum: 1a65
• PubMed: 9546223
• UniProt: Q9Y780