Structure of PDB 4jhu Chain A

Receptor sequence

>4jhuA (length=496) Species: 195176 (Cerrena caperata)

GIGPVTDLTISDGPVSPDGFTRQAILVNNQFPSPLITGNKGDRFQLNVID
NMNNHTMLKSTSIHWHGFFQHGTNWADGPAFVNQCPISPGHSFLYDFQVP
DQAGTFWYHSHLSTQYCDGLRGPIVVYDPQDPHKDLYDVDDDSTVITLAD
WYHLAAKVGPAVPTADATLINGLGRSISTLNADLAVISVTKGKRYRFRLV
SLSCDPNHTFSIDGHTMTVIEADSVNLKPQVVDSIQIFAAQRYSFVLNAD
QDIGNYWIRAMPNSGTRNFDGGVNSAILRYDGADPVEPTTTQTPSSQPLV
ESALTTLEGTAAPGSPTAGGVDLAINMAFGFAGGRFTINGASFTPPTVPV
LLQILSGAQNAQDLLPTGSVYSLPANADIEISLPATAAAPGFPHPFHLHG
HTFAVVRSAGSSTYNYANPVYRDVVSTGSPGDNVTIRFRTDNPGPWFLHC
HIDFHLEAGFAVVMAEDIPDVAAVNPVPQAWSDLCPTYNALDPNDQ

3D structure

• PDB: 4jhu Elucidation of the crystal structure of Coriolopsis caperata laccase: restoration of the structure and activity of the native enzyme from the T2-depleted form by copper ions.
• Chain: A
• Resolution: 1.89 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	CU	A	H111 H399 H449	H111 H399 H449
BS02	CU	A	H66 H109 H451	H66 H109 H451
BS03	CU	A	H394 C450 H455	H394 C450 H455
BS04	CU	A	H64 H397 H399	H64 H397 H399
BS05	CU	A	H401 D441	H401 D441

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:4jhu, PDBe:4jhu, PDBj:4jhu
• PDBsum: 4jhu
• PubMed: 25849396
• UniProt: M1GME7