Structure of PDB 4a2g Chain A

Receptor sequence
>4a2gA (length=496) Species: 76126 (Coriolopsis gallica) [Search protein sequence]
AIGPVADLTISNGAVSPDGFSRQAILVNDVFPSPLITGNKGDRFQLNVID
NMTNHTMLKSTSIHWHGFFQHGTNWADGPAFVNQCPISTGHAFLYDFQVP
DQAGTFWYHSHLSTQYCDGLRGPIVVYDPNDPHASLYDVDDDSTVITLAD
WYHLAAKVGAPVPTADATLINGLGRSAATLAADLAVITVTKGKRYRFRLV
SLSCDPNYTFSIDGHSLTVIEADSVNLKPHTVDSLQIFAAQRYSFVLNAD
QDVDNYWIRALPNSGTQNFAGGTNSAILRYDGAAPVEPTTSQTPSTNPLV
ESALTTLKGTAAPGSPTPGGVDLALNMAFGFAGGNFTINGASFTPPTVPV
LLQILSGAQSAADLLPAGSVYSLPANADIEISLPATAAAPGFPHPFHLHG
HVFAVVRSAGSSTYNYANPVYRDVVSTGAPGDNVTIRFRTDNPGPWFLHC
HIDFHLEAGFAVVMAEDIPDVAATNPVPQAWSDLCPTYDALSPDDQ
3D structure
PDB4a2g Structural Changes Caused by Radiation-Induced Reduction and Radiolysis: The Effect of X-Ray Absorbed Dose in a Fungal Multicopper Oxidase
ChainA
Resolution1.8 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) H85 H87 H130 H132 H415 H418 H420 H470 C471 H472 I473 H476 F481
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 H87 H130 H472 H66 H109 H451
BS02 CU A H132 H420 H470 H111 H399 H449
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:4a2g, PDBe:4a2g, PDBj:4a2g
PDBsum4a2g
PubMed22525754
UniProtQ1W6B1

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