Structure of PDB 6i3k Chain A

Receptor sequence
>6i3kA (length=534) Species: 1859699 (Albifimbria verrucaria) [Search protein sequence]
VAQISPQYPMFTVPLPIPPVKQPRLTVTNPVNGQEIWYYEVEIKPFTHQV
YPDLGSADLVGYDGMSPGPTFQVPRGVETVVRFINNAEAPNSVHLHGSFS
RAAFDGWAEDITEPGSFKDYYYPNRQSARTLWYHDHAMHITAENAYRGQA
GLYMLTDPAEDALNLPSGYGEFDIPMILTSKQYTANGNLVTTNGELNSFW
GDVIHVNGQPWPFKNVEPRKYRFRFLDAAVSRSFGLYFADTDAIDTRLPF
KVIASDSGLLEHPADTSLLYISMAERYEVVFDFSDYAGKTIELRNLGGSI
GGIGTDTDYDNTDKVMRFVVADDTTQPDTSVVPANLRDVPFPSPTTNTPR
QFRFGRTGPTWTINGVAFADVQNRLLANVPVGTVERWELINAGNGATHPI
HIHLVDFKVISRTSGNNARTVMPYESGLKDVVWLGRRETVVVEAHYAPFP
GVYMFHCHNLIHEDHDMMAAFNATVLPDYGYNATVFVDPMEELWQARPYE
LGEFQAQSGQFSVQAVTERIQTMAEYRPYAAADE
3D structure
PDB6i3k Trp-His covalent adduct in bilirubin oxidase is crucial for effective bilirubin binding but has a minor role in electron transfer.
ChainA
Resolution1.6 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 1.3.3.5: bilirubin oxidase.
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 H398 C457 H462 H398 C457 H462
BS02 CU A H136 H403 H456 H136 H403 H456
BS03 CU A H96 H134 H458 H96 H134 H458
BS04 CU A H94 H401 H403 H94 H401 H403
BS05 FC6 A R356 G393 N394 G395 R356 G393 N394 G395
Gene Ontology
Molecular Function
GO:0005507 copper ion binding
GO:0016491 oxidoreductase activity
GO:0046872 metal ion binding
GO:0047705 bilirubin oxidase activity

View graph for
Molecular Function
External links
PDB RCSB:6i3k, PDBe:6i3k, PDBj:6i3k
PDBsum6i3k
PubMed31548583
UniProtQ12737|BLRO_ALBVE Bilirubin oxidase

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