Structure of PDB 4a66 Chain A

Receptor sequence
>4a66A (length=501) Species: 1423 (Bacillus subtilis) [Search protein sequence]
TLEKFVDALPIPDTLKPVQQSKEKTYYEVTMEECTHQLHRDLPPTRLWGY
NGLFPGPTIEVKRNENVYVKWMNNLPSTHFLPIDHTIHHEEPEVKTVVHL
HGGVTPDDSAGYPEAWFSKDFEQTGPYFKREVYHYPNQQRGAILWYHDHA
MALTRLNVYAGLVGAYIIHDPKEKRLKLPSDEYDVPLLITDRTINEDGSL
FYPSAPENPSPSLPNPSIVPAFCGETILVNGKVWPYLEVEPRKYRFRVIN
ASNTRTYNLSLDNGGDFIQIGSDGGLLPRSVKLNSFSLAPAERYDIIIDF
TAYEGESIILANSAGCGGDVNPETDANIMQFRVTKPLAQKDESRKPKYLA
SYPERIQNIRTLKLAGTQDEYGRPVLLLNNKRWHDPVTETPKVGTTEIWS
IINPTRGTHPIHLHLVSFRVLDRRPFDIARYQESGELSYTGPAVPPPPSE
KGWKDTIQAHAGEVLRIAATFGPYSGRYVWHCHILEHEDYDMMRPMDITD
P
3D structure
PDB4a66 The Role of Asp116 in the Reductive Cleavage of Dioxygen to Water in Cota Laccase: Assistance During the Proton Transfer Mechanism
ChainA
Resolution1.95 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 H409 C482 H487
BS02 CU A H107 H153 H493 H101 H147 H483
BS03 CU A H155 H424 H491 H149 H414 H481
BS04 CU A H105 H422 H424 H99 H412 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:4a66, PDBe:4a66, PDBj:4a66
PDBsum4a66
PubMed22281748
UniProtP07788|COTA_BACSU Laccase (Gene Name=cotA)

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