Structure of PDB 2yaq Chain A

Receptor sequence

>2yaqA (length=439) Species: 262724 (Thermus thermophilus HB27)

GPSFPEPKVVRSQGGLLSLKLSATPTPLAIAGQRATLLTYGGSFPGPTLR
VRPRDTVRLTLENRLPEPTNLHWHGLPISPKVDDPFLEIPPGESWTYEFT
VPKELAGTFWYHPHLHGRVAPQLFAGLLGALVVESSLDAIPELREAEEHL
LVLKDLALQGGRPAPHTPMDWMNGKEGDLVLVNGALRPTLVAQKATLRLR
LLNASNARYYRLALQDHPLYLIAADGGFLEEPLEVSELLLAPGERAEVLV
RLRKEGRFLLQALPYDRGAMGMMDMGGMAHAMPQGPSRPETLLYLIAPKN
PKPLPLPKALSPFPTLPAPVVTRRLVLTEDMMAARFFINGQVFDHRRVDL
KGQAQTVEVWEVENQGDMDHPFHLHVHPFQVLSVGGRPFPYRAWKDVVNL
KAGEVARLLVPLREKGRTVFHCHIVEHEDRGMMGVLEVG

3D structure

• PDB: 2yaq X-Ray-Induced Catalytic Active-Site Reduction of a Multicopper Oxidase: Structural Insights Into the Proton-Relay Mechanism and O2-Reduction States.
• Chain: A
• Resolution: 1.8 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): H95 H97 H135 H137 H393 H396 H398 H444 C445 H446 I447 H450 M455
• Catalytic site (residue number reindexed from 1): H72 H74 H112 H114 H370 H373 H375 H421 C422 H423 I424 H427 M432
• 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	H393 C445 H450	H370 C422 H427
BS02	CU	A	H97 H135 H446	H74 H112 H423
BS03	CU	A	H137 H398 H444	H114 H375 H421

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:0030288 outer membrane-bounded periplasmic space

External links

• PDB: RCSB:2yaq, PDBe:2yaq, PDBj:2yaq
• PDBsum: 2yaq
• PubMed: 26627648
• UniProt: Q72HW2