Structure of PDB 4q89 Chain B

Receptor sequence
>4q89B (length=499) Species: 224308 (Bacillus subtilis subsp. subtilis str. 168) [Search protein sequence]
TLEKFVDALPIPDTLKPVQQSKEKTYYEVTMEECTHQLHRDLPPTRLWGY
NGLFPGPTIEVKRNENVYVKWMNNLPSTHFLPIDHTIHEEPEVKTVVHLH
GGVTPDDSDGYPEAWFSKDFEQTGPYFKREVYHYPNQQRGAILWYHDHAM
ALTRLNVYAGLVGAYIIHDPKEKRLKLPSDEYDVPLLITDRTINEDGSLF
YPSAPENPSPSLPNPSIVPAFCGETILVNGKVWPYLEVEPRKYRFRVINA
SNTRTYNLSLDNGGDFIQIGSDGGLLPRSVKLNSFSLAPAERYDIIIDFT
AYEGESIILANSAGCGGDVNPETDANIMQFRVTKPLAQKDESRKPKYLAS
YPRIQNIRTLKLAGTQDEYGRPVLLLNNKRWHDPVTETPKVGTTEIWSII
NPTRGTHPIHLHLVSFRVLDRRPFDIARYQESGELSYTGPAVPPPPSEKG
WKDTIQAHAGEVLRIAATFGPYSGRYVWHCHILEHEDYDMMRPMDITDP
3D structure
PDB4q89 The crystal structure of CotA laccase complexed with sinapic acid
ChainB
Resolution2.31 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 B H419 C492 H497 H407 C480 H485
BS02 CU B H105 H422 H424 H98 H410 H412
BS03 CU B H155 H424 H491 H148 H412 H479
BS04 CU B H107 H153 H493 H100 H146 H481
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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Cellular Component
External links
PDB RCSB:4q89, PDBe:4q89, PDBj:4q89
PDBsum4q89
PubMed
UniProtP07788|COTA_BACSU Laccase (Gene Name=cotA)

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