Structure of PDB 6rhp Chain A

Receptor sequence
>6rhpA (length=497) Species: 627145 (Steccherinum murashkinskyi) [Search protein sequence]
AQIGPVTDLHITNANISPDGFSRPAVLAGGTFPGPTIAGNTGDNFQITVF
NDLTDPSMLTDTSIHWHGLFQKGTNWADGPAFVTQCPIITGQSFDYNFNV
PGQAGTFWYHSHLSTQYCDGLRGPFVVYDPNDPNASLYDVDDDTTIITLA
DWYHTLAQQEPIGAAITADATLINGLGRSFTNTTASPLSVITVQSGKRYR
MRLVSISCDPNYLFSIDGHDMTIIEVDGVNSQQLTVDQIQIFAAQRYSFV
LNANQPVGNYWIRAQPNSGGQGFDGGINSAILRYEGATVEDPTTTAPTTF
SNPLVETDLHPLADLGVPGQPFRGGADDPLVLNLAFANGRFSIDGVSFVP
PTVPVLLQILSGAQNAQDLLPAGSVISLPSNSVIEVALPAGAAGGPHPFH
LHGHNFAVVQSANNATPNYVNPIWRDTVSIGGTGDNVTIRFTTNNPGPWF
LHCHIDWHLEAGFAIVFAEDIPDTASANPVPQAWSDLCPAYDQAHNI
3D structure
PDB6rhp The subatomic resolution study of laccase inhibition by chloride and fluoride anions using single-crystal serial crystallography: insights into the enzymatic reaction mechanism.
ChainA
Resolution1.6 Å
3D
structure
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Enzymatic activity
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
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

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Molecular Function
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Cellular Component
External links
PDB RCSB:6rhp, PDBe:6rhp, PDBj:6rhp
PDBsum6rhp
PubMed31478903
UniProtI1VE66

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