Structure of PDB 4jhv Chain A

Receptor sequence
>4jhvA (length=496) Species: 195176 (Cerrena caperata) [Search protein sequence]
GIGPVTDLTISDGPVSPDGFTRQAILVNNQFPSPLITGNKGDRFQLNVID
NMNNHTMLKSTSIHWHGFFQHGTNWADGPAFVNQCPISPGHSFLYDFQVP
DQAGTFWYHSHLSTQYCDGLRGPIVVYDPQDPHKDLYDVDDDSTVITLAD
WYHLAAKVGPAVPTADATLINGLGRSISTLNADLAVISVTKGKRYRFRLV
SLSCDPNHTFSIDGHTMTVIEADSVNLKPQVVDSIQIFAAQRYSFVLNAD
QDIGNYWIRAMPNSGTRNFDGGVNSAILRYDGADPVEPTTTQTPSSQPLV
ESALTTLEGTAAPGSPTAGGVDLAINMAFGFAGGRFTINGASFTPPTVPV
LLQILSGAQNAQDLLPTGSVYSLPANADIEISLPATAAAPGFPHPFHLHG
HTFAVVRSAGSSTYNYANPVYRDVVSTGSPGDNVTIRFRTDNPGPWFLHC
HIDFHLEAGFAVVMAEDIPDVAAVNPVPQAWSDLCPTYNALDPNDQ
3D structure
PDB4jhv 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.
ChainA
Resolution1.6 Å
3D
structure
Catalytic site residues are labeled in the structure
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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 H64 H397
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

View graph for
Molecular Function
View graph for
Cellular Component
External links
PDB RCSB:4jhv, PDBe:4jhv, PDBj:4jhv
PDBsum4jhv
PubMed25849396
UniProtM1GME7

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