Structure of PDB 2qt6 Chain A

Receptor sequence

>2qt6A (length=498) Species: 5365 (Lentinus tigrinus)

AVGPVADLTVTNANIVPDGFERAAIVVNNVFPAPLITGNMGDNFQLNLVN
QMTNHTMLKTTSIHWHGFFQKGTNWADGPAFINQCPIASGNSFLYDFQVP
GQAGTFWYHSHLSTQYCDGLRGPFVVYDPNDPHANLYDVDDESTVITLAD
WYHVAAKLGPRFPKGADSTLINGLGRSTSTPTADLAVISVTKGKRYRFRL
VSLSCDPNYTFSIDSHQLTVIEADGVSTQPVTVDSIQIFAAQRYSFVLNA
NQDVDNYWIRANPNFGTTGFADGVNSAILRYDDADPVEPVTNQTGTTLLL
ETDLHPLTSMPVPGNPTQGGADLNLNMAFNFDGTNFFINGESFTPPTVPV
LLQIISGANTAQDLLPSGSVYSLPSNSSIEITFPATTAAPGAPHPFHLHG
HVFAVVRSAGSTSYNYDDPVWRDVVSTGTPQAGDNVTIRFQTDNPGPWFL
HCHIDFHLDAGFAVVMAEDIPNTVNANPVPQAWSNLCPTYDALEPSNE

3D structure

• PDB: 2qt6 Crystal structure of a blue laccase from Lentinus tigrinus: evidences for intermediates in the molecular oxygen reductive splitting by multicopper oxidases.
• Chain: A
• Resolution: 1.5 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): H64 H66 H109 H111 H394 H397 H399 H451 C452 H453 I454 H457 F462
• Catalytic site (residue number reindexed from 1): H64 H66 H109 H111 H394 H397 H399 H451 C452 H453 I454 H457 F462
• 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	H394 C452 H457	H394 C452 H457
BS02	CU	A	H64 H397 H399	H64 H397 H399
BS03	CU	A	H111 H399 H451	H111 H399 H451
BS04	CU	A	H66 H109 H453	H66 H109 H453
BS05	CA	A	D469 N472	D469 N472
BS06	CA	A	E341 S367	E341 S367

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:2qt6, PDBe:2qt6, PDBj:2qt6
• PDBsum: 2qt6
• PubMed: 17897461
• UniProt: Q5EBY5