Structure of PDB 4ako Chain A

Receptor sequence
>4akoA (length=506) Species: 1423 (Bacillus subtilis) [Search protein sequence]
TLEKFVDALPIPDTLKPVQQSKEKTYYEVTMEECTHQLHRDLPPTRLWGY
NGLFPGPTIEVKRNENVYVKWMNNLPSTHFLPIDHTIHHSEEPEVKTVVH
LHGGVTPDDSDGYPEAWFSKDFEQTGPYFKREVYHYPNQQRGAILWYHDH
AMALTRLNVYAGLVGAYIIHDPKEKRLKLPSDEYDVPLLITDRTINEDGS
LFYPSAPENPSPSLPNPSIVPAFCGETILVNGKVWPYLEVEPRKYRFRVI
NASNTRTYNLSLDNGGDFIQIGSDGGLLPRSVKLNSFSLAPAERYDIIID
FTAYEGESIILANSAGCGGDVNPETDANIMQFRVTKPLAQKDESRKPKYL
ASYPSVQHERIQNIRTLKLAGTQDEYGRPVLLLNNKRWHDPVTETPKVGT
TEIWSIINPTRGTHPIHLHLVSFRVLDRRPFDIARYQESGELSYTGPAVP
PPPSEKGWKDTIQAHAGEVLRIAATFGPYSGRYVWHCHILEHLDYDMMRP
MDITDP
3D structure
PDB4ako The Role of Glu498 in the Dioxygen Reactivity of Cota-Laccase from Bacillus Subtilis.
ChainA
Resolution1.7 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 H414 C487 H492
BS02 CU A H107 H153 H493 H102 H148 H488
BS03 CU A H155 H424 H491 H150 H419 H486
BS04 CU A H105 H422 H424 H100 H417 H419
BS05 OXY A H105 H153 H155 H491 H493 H100 H148 H150 H486 H488
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:4ako, PDBe:4ako, PDBj:4ako
PDBsum4ako
PubMed20200715
UniProtP07788|COTA_BACSU Laccase (Gene Name=cotA)

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