Structure of PDB 4akq Chain A

Receptor sequence
>4akqA (length=505) Species: 1423 (Bacillus subtilis) [Search protein sequence]
TLEKFVDALPIPDTLKPVQQSKEKTYYEVTMEECTHQLHRDLPPTRLWGY
NGLFPGPTIEVKRNENVYVKWMNNLPSTHFLPIDHTIHHEEPEVKTVVHL
HGGVTPDDSDGYPEAWFSKDFEQTGPYFKREVYHYPNQQRGAILWYHDHA
MALTRLNVYAGLVGAYIIHDPKEKRLKLPSDEYDVPLLITDRTINEDGSL
FYPSAPENPSPSLPNPSIVPAFCGETILVNGKVWPYLEVEPRKYRFRVIN
ASNTRTYNLSLDNGGDFIQIGSDGGLLPRSVKLNSFSLAPAERYDIIIDF
TAYEGESIILANSAGCGGDVNPETDANIMQFRVTKPLAQKDESRKPKYLA
SYPSVQHERIQNIRTLKLAGTQDEYGRPVLLLNNKRWHDPVTETPKVGTT
EIWSIINPTRGTHPIHLHLVSFRVLDRRPFDIARYQESGELSYTGPAVPP
PPSEKGWKDTIQAHAGEVLRIAATFGPYSGRYVWHCHILEHDDYDMMRPM
DITDP
3D structure
PDB4akq The Role of Glu498 in the Dioxygen Reactivity of Cota-Laccase from Bacillus Subtilis.
ChainA
Resolution2.1 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 H413 C486 H491
BS02 CU A H107 H153 H493 H101 H147 H487
BS03 CU A H155 H424 H491 H149 H418 H485
BS04 CU A H105 H422 H424 H99 H416 H418
BS05 OXY A H105 H153 H155 H422 H491 H493 H99 H147 H149 H416 H485 H487
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:4akq, PDBe:4akq, PDBj:4akq
PDBsum4akq
PubMed20200715
UniProtP07788|COTA_BACSU Laccase (Gene Name=cotA)

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