Structure of PDB 2hrg Chain A

Receptor sequence

>2hrgA (length=496) Species: 76130 (Coriolopsis trogii)

AIGPVADLTISNGAVSPDGFSRQAILVNDVFPSPLITGNKGDRFQLNVID
NMTNHTMLKSTSIHWHGFFQHGTNWADGPAFVNQCPISTGHAFLYDFQVP
DQAGTFWYHSHLSTQYCDGLRGPIVVYDPQDPHKSLYDVDDDSTVITLAD
WYHLAAKVGSPVPTADATLINGLGRSIDTLNADLAVITVTKGKRYRFRLV
SLSCDPNHVFSIDGHSLTVIEADSVNLKPQTVDSIQIFAAQRYSFVLNAD
QDVGNYWIRALPNSGTRNFDGGVNSAILRYDGAAPVEPTTSQTPSTNPLV
ESALTTLEGTAAPGSPAPGGVDLALNMAFGFAGGKFTINGASFTPPTVPV
LLQILSGAQSAQDLLPSGSVYSLPANADIEISLPATAAAPGFPHPFHLHG
HTFAVVRSAGSSTYNYENPVYRDVVSTGSPGDNVTIRFRTDNPGPWFLHC
HIDFHLEAGFAVVMAEDIPEVAATNPVPQAWSDLCPTYDALSPDDQ

3D structure

• PDB: 2hrg Crystal structure of the blue multicopper oxidase from the white-rot fungus Trametes trogii complexed with p-toluate
• Chain: A
• Resolution: 1.58 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): H64 H66 H109 H111 H394 H397 H399 H449 C450 H451 I452 H455 F460
• 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	CA	A	S143 T188	S143 T188
BS02	CA	A	A103 S224	A103 S224
BS03	CU	A	H394 C450 H455	H394 C450 H455
BS04	CU	A	H66 H109 H451	H66 H109 H451
BS05	CU	A	H64 H397 H399	H64 H397 H399
BS06	CU	A	H111 H399 H449	H111 H399 H449
BS07	4MA	A	V162 F331 P390 G391 H455	V162 F331 P390 G391 H455

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:2hrg, PDBe:2hrg, PDBj:2hrg
• PDBsum: 2hrg
• UniProt: Q9HDQ0