Structure of PDB 1hfu Chain A

Receptor sequence

>1hfuA (length=500) Species: 5346 (Coprinopsis cinerea)

AIVNSVDTMTLTNANVSPDGFTRAGILVNGVHGPLIRGGKNDNFELNVVN
DLDNPTMLRPTSIHWHGLFQRGTNWADGADGVNQCPISPGHAFLYKFTPA
GHAGTFWYHSHFGTQYCDGLRGPMVIYDDNDPHAALYDEDDENTIITLAD
WYHIPAPSIQQPDATLINGKGRYVGGPAAELSIVNVEQGKKYRMRLISLS
CDPNWQFSIDGHELTIIEVDGELTEPHTVDRLQIFTGQRYSFVLDANQPV
DNYWIRAQPNKGRNGLAGTFANGVNSAILRYAGAANADPTTSANPNPAQL
NEADLHALIDPAAPGIPTPGAADVNLRFQLGFSGGRFTINGTAYESPSVP
TLLQIMSGAQSANDLLPAGSVYELPRNQVVELVVPAGVLGGPHPFHLHGH
AFSVVRSAGSSTYNFVNPVKRDVVSLGVTGDEVTIRFVTDNPGPWFFHCH
IEFHLMNGLAIVFAEDMANTVDANNPPVEWAQLCEIYDDLPPEATSIQTV

3D structure

• PDB: 1hfu Structure of the Laccase from Coprinus Cinereus at 1.68A Resolution: Evidence for Different Type 2 Cu-Depleted Isoforms
• Chain: A
• Resolution: 1.68 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 H393 H396 H398 H448 C449 H450 I451 H454 L459
• 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	MAN	A	P157 I500 T502	P157 I497 T499
BS02	CU	A	H396 C452 H457	H393 C449 H454
BS03	CU	A	H111 H401 H451	H111 H398 H448
BS04	CU	A	H66 H109 H453	H66 H109 H450

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:1hfu, PDBe:1hfu, PDBj:1hfu
• PDBsum: 1hfu
• PubMed: 11173497
• UniProt: Q9Y780