Structure of PDB 5zlj Chain A

Receptor sequence
>5zljA (length=503) Species: 224308 (Bacillus subtilis subsp. subtilis str. 168) [Search protein sequence]
TLEKFVDALPIPDTLKPVQQSKEKTYYEVTMEECTHQLHRDLPPTRLWGY
NGLFPGPTIEVKRNENVYVKWMNNLPSTHFLPIDHTIHHSHEEPEVKTVV
HLHGGVTPDDSDGYPEAWFSKDFEQTGPYFKREVYHYPNQQRGAILWYHD
HAMALTRLNVYAGLVGAYIIHDPKEKRLKLPSDEYDVPLLITDRTINEDG
SLFYPSAPENPSPSLPNPSIVPAFCGETILVNGKVWPYLEVEPRKYRFRV
INASNTRTYNLSLDNGGDFIQIGSDGGLLPRSVKLNSFSLAPAERYDIII
DFTAYEGESIILANSAGCGGDVNPETDANIMQFRVTKPLAQKDESRKPKY
LASYPERIQNIRTLKLAGTQDEYGRPVLLLNNKRWHDPVTETPKVGTTEI
WSIINPTRGTHPIHLHLVSFRVLDRRPFDIARYQESGELSYTGPAVPPPP
SEKGWKDTIQAHAGEVLRIAATFGPYSGRYVWHCHILEHEDYDMMRPMDI
TDP
3D structure
PDB5zlj Structural Insight into the Allosteric Coupling of Cu1 Site and Trinuclear Cu Cluster in CotA Laccase.
ChainA
Resolution1.96 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 1.10.3.2: laccase.
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 H419 C492 H497 H411 C484 H489
BS02 CU A H105 H422 H424 H101 H414 H416
BS03 CU A H155 H424 H491 H151 H416 H483
BS04 CU A H107 H153 H493 H103 H149 H485
Gene Ontology
Molecular Function
GO:0005507 copper ion binding
GO:0016491 oxidoreductase activity
GO:0046872 metal ion binding
Biological Process
GO:0030435 sporulation resulting in formation of a cellular spore
Cellular Component
GO:0030288 outer membrane-bounded periplasmic space

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:5zlj, PDBe:5zlj, PDBj:5zlj
PDBsum5zlj
PubMed29722464
UniProtP07788|COTA_BACSU Laccase (Gene Name=cotA)

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