Structure of PDB 4a66 Chain A Binding Site BS02

Receptor Information

>4a66 Chain A (length=501) Species: 1423 (Bacillus subtilis)

TLEKFVDALPIPDTLKPVQQSKEKTYYEVTMEECTHQLHRDLPPTRLWGY
NGLFPGPTIEVKRNENVYVKWMNNLPSTHFLPIDHTIHHEEPEVKTVVHL
HGGVTPDDSAGYPEAWFSKDFEQTGPYFKREVYHYPNQQRGAILWYHDHA
MALTRLNVYAGLVGAYIIHDPKEKRLKLPSDEYDVPLLITDRTINEDGSL
FYPSAPENPSPSLPNPSIVPAFCGETILVNGKVWPYLEVEPRKYRFRVIN
ASNTRTYNLSLDNGGDFIQIGSDGGLLPRSVKLNSFSLAPAERYDIIIDF
TAYEGESIILANSAGCGGDVNPETDANIMQFRVTKPLAQKDESRKPKYLA
SYPERIQNIRTLKLAGTQDEYGRPVLLLNNKRWHDPVTETPKVGTTEIWS
IINPTRGTHPIHLHLVSFRVLDRRPFDIARYQESGELSYTGPAVPPPPSE
KGWKDTIQAHAGEVLRIAATFGPYSGRYVWHCHILEHEDYDMMRPMDITD
P

Ligand information

• Ligand ID: CU
• InChI: InChI=1S/Cu/q+2
• InChIKey: JPVYNHNXODAKFH-UHFFFAOYSA-N
• SMILES:
  ACDLabs 10.04
  OpenEye OEToolkits 1.5.0: [Cu+2]
  CACTVS 3.341: [Cu++]
• Formula: Cu
• Name: COPPER (II) ION
• DrugBank: DB14552
• PDB chain: 4a66 Chain A Residue 1513

Receptor-Ligand Complex Structure

Structure summary

• PDB: 4a66 The Role of Asp116 in the Reductive Cleavage of Dioxygen to Water in Cota Laccase: Assistance During the Proton Transfer Mechanism
• Resolution: 1.95 Å
• Binding residue (original residue number in PDB): H107 H153 H493
• Binding residue (residue number reindexed from 1): H101 H147 H483
• Annotation score: 1

Enzymatic activity

• Enzyme Commision number: 1.10.3.2: laccase.
  1.3.3.5: bilirubin oxidase.

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

External links

• PDB: RCSB:4a66, PDBe:4a66, PDBj:4a66
• PDBsum: 4a66
• PubMed: 22281748
• UniProt: P07788|COTA_BACSU Laccase (Gene Name=cotA)