Structure of PDB 5mhu Chain A

Receptor sequence

>5mhuA (length=499) Species: 627145 (Steccherinum murashkinskyi)

AQIGPVTDLHITNANISPDGFSRPAVLAGGTFPGPTIAGNTGDNFQITVF
NDLTDPSMLTDTSIHWHGLFQKGTNWADGPAFVTQCPIITGQSFDYNFNV
PGQAGTFWYHSHLSTQYCDGLRGPFVVYDPNDPNASLYDVDDDTTIITLA
DWYHTLAQQEPIGAAITADATLINGLGRSFTNTTASPLSVITVQSGKRYR
MRLVSISCDPNYLFSIDGHDMTIIEVDGVNSQQLTVDQIQIFAAQRYSFV
LNANQPVGNYWIRAQPNSGGQGFDGGINSAILRYEGATVEDPTTTAPTTF
SNPLVETDLHPLADLGVPGQPFRGGADDPLVLNLAFANGRFSIDGVSFVP
PTVPVLLQILSGAQNAQDLLPAGSVISLPSNSVIEVALPAGAAGGPHPFH
LHGHNFAVVQSANNATPNYVNPIWRDTVSIGGTGDNVTIRFTTNNPGPWF
LHCHIDWHLEAGFAIVFAEDIPDTASANPVPQAWSDLCPAYDQAHNIST

3D structure

• PDB: 5mhu Structural study of the X-ray-induced enzymatic reduction of molecular oxygen to water by Steccherinum murashkinskyi laccase: insights into the reaction mechanism.
• Chain: A
• Resolution: 1.35 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): H65 H67 H110 H112 H397 H400 H402 H452 C453 H454 I455 H458 F463
• Catalytic site (residue number reindexed from 1): H65 H67 H110 H112 H397 H400 H402 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	CU	A	H112 H402 H452	H112 H402 H452
BS02	CU	A	H67 H110 H454	H67 H110 H454
BS03	CU	A	H65 H400	H65 H400
BS04	CU	A	H397 C453 H458	H397 C453 H458
BS05	OXY	A	H65 H110 H112 H452 H454	H65 H110 H112 H452 H454
BS06	OXY	A	H110 D456	H110 D456

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:5mhu, PDBe:5mhu, PDBj:5mhu
• PDBsum: 5mhu
• PubMed: 28471364
• UniProt: I1VE66