Structure of PDB 3div Chain A

Receptor sequence

>3divA (length=499) Species: 90311 (Cerrena)

AVGPVADNTITDAATSPDGFSRQAVVVNGVTPGPLVAGNIGDRFQLNVID
NLTNHTMLKTTSVHWHGFFQQGTNWADGPAFINQCPISPGHSFLYDFQVP
NQAGTFWYHSHLSTQYCDGLRGPFVVYDPNDPHASRYDVDNDDTVITLAD
WYHTAAKLGPRFPAGADATLINGKGRAPSDTSAELSVIKVTKGKRYRFRL
VSLSCDPNFTFSIDGHNLTIIEVDSSNSQPLSVDSIQIFAAQRYSFVLNA
NQAVDNYWIRANPNFGNVGFNGGINSAILRYDGAPAVEPTTNQTTSVKPL
NEVNLHPLVSTPVPGSPSSGGVDKAINMAFNFNGSNFFINGASFVPPSVP
VLLQILSGAQTAQDLLPSGSVYVLPSNASIEISFPATAAAPGAPHPFHLH
GHTFAVVRSAGSTVYNYSNPIFRDVVSTGTPAAGDNVTIRFLTNNPGPWF
LHCHIDFHLEGGFAVVQAEDVPDVKATNPVPQAWSDLCPTYDANAPSDQ

3D structure

• PDB: 3div Crystal Structure of laccase from Cerrena maxima at 1.76A resolution.
• Chain: A
• Resolution: 1.76 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): H64 H66 H109 H111 H395 H398 H400 H452 C453 H454 I455 H458 F463
• Catalytic site (residue number reindexed from 1): H64 H66 H109 H111 H395 H398 H400 H452 C453 H454 I455 H458 F463
• 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	F20 S21	F20 S21
BS02	CU	A	H111 H400 H452	H111 H400 H452
BS03	CU	A	H66 H109 H454	H66 H109 H454
BS04	CU	A	H64 H66 H398 H400	H64 H66 H398 H400
BS05	CU	A	H395 C453 H458	H395 C453 H458

Gene Ontology

Molecular Function

• GO:0005507 copper ion binding
• GO:0016491 oxidoreductase activity
• GO:0046872 metal ion binding
• GO:0052716 hydroquinone:oxygen oxidoreductase activity

Biological Process

• GO:0046274 lignin catabolic process

Cellular Component

• GO:0005576 extracellular region

External links

• PDB: RCSB:3div, PDBe:3div, PDBj:3div
• PDBsum: 3div
• UniProt: D0VWU3|LAC1_TRAMX Laccase