Structure of PDB 4q89 Chain A

Receptor sequence
>4q89A (length=501) Species: 224308 (Bacillus subtilis subsp. subtilis str. 168) [Search protein sequence]
MTLEKFVDALPIPDTLKPVQQSKEKTYYEVTMEECTHQLHRDLPPTRLWG
YNGLFPGPTIEVKRNENVYVKWMNNLPSTHFLPIDHTIHQHEEPEVKTVV
HLHGGVTPDDSDGYPEAWFSKDFEQTGPYFKREVYHYPNQQRGAILWYHD
HAMALTRLNVYAGLVGAYIIHDPKEKRLKLPSDEYDVPLLITDRTINEDG
SLFYPSAPENPSPSLPNPSIVPAFCGETILVNGKVWPYLEVEPRKYRFRV
INASNTRTYNLSLDNGGDFIQIGSDGGLLPRSVKLNSFSLAPAERYDIII
DFTAYEGESIILANSAGCGGDVNPETDANIMQFRVTKPLAQKDESRKPKY
LASYIQNIRTLKLAGTQDEYGRPVLLLNNKRWHDPVTETPKVGTTEIWSI
INPTRGTHPIHLHLVSFRVLDRRPFDIARYQESGELSYTGPAVPPPPSEK
GWKDTIQAHAGEVLRIAATFGPYSGRYVWHCHILEHEDYDMMRPMDITDP
H
3D structure
PDB4q89 The crystal structure of CotA laccase complexed with sinapic acid
ChainA
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 A H419 C492 H497 H408 C481 H486
BS02 CU A H105 H422 H424 H101 H411 H413
BS03 CU A H155 H424 H491 H151 H413 H480
BS04 CU A H107 H153 H493 H103 H149 H482
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:4q89, PDBe:4q89, PDBj:4q89
PDBsum4q89
PubMed
UniProtP07788|COTA_BACSU Laccase (Gene Name=cotA)

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