Structure of PDB 5zll Chain A

Receptor sequence
>5zllA (length=503) Species: 224308 (Bacillus subtilis subsp. subtilis str. 168) [Search protein sequence]
TLEKFVDALPIPDTLKPVQQSKEKTYYEVTMEECTHQLHRDLPPTRLWGY
NGLFPGPTIEVKRNENVYVKWMNNLPSTHFLPIDHTIHHSHEEPEVKTVV
HLHGGVTPDDSDGYPEAWFSKDFEQTGPYFKREVYHYPNQQRGAILWYHD
HAMALTRLNVYAGLVGAYIIHDPKEKRLKLPSDEYDVPLLITDRTINEDG
SLFYPSAPENPSPSLPNPSIVPAFCGETILVNGKVWPYLEVEPRKYRFRV
INASNTRTYNLSLDNGGDFIQIGSDGGLLPRSVKLNSFSLAPAERYDIII
DFTAYEGESIILANSAGCGGDVNPETDANIMQFRVTKPLAQKDESRKPKY
LASYHERIQNIRTLKLAGTQDEYGRPVLLLNNKRWHDPVTETPKVGTTEI
WSIINPTRGTHPIHLHLVSFRVLDRRPFDIARYQESGELSYTGPAVPPPP
SEKGWKDTIQAHAGEVLRIAATFGPYSGRYVWHCCILEHEDYDMMRPMDI
TDP
3D structure
PDB5zll Structural Insight into the Allosteric Coupling of Cu1 Site and Trinuclear Cu Cluster in CotA Laccase.
ChainA
Resolution2.6 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 H155 H424 H491 H151 H416 H483
BS03 CU A H105 H107 H422 H101 H103 H414
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:5zll, PDBe:5zll, PDBj:5zll
PDBsum5zll
PubMed29722464
UniProtP07788|COTA_BACSU Laccase (Gene Name=cotA)

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