Structure of PDB 2bhf Chain A

Receptor sequence
>2bhfA (length=504) Species: 1423 (Bacillus subtilis) [Search protein sequence]
TLEKFVDALPIPDTLKPVQQSKEKTYYEVTMEECTHQLHRDLPPTRLWGY
NGLFPGPTIEVKRNENVYVKWMNNLPSTHFLPIDHTIHEEPEVKTVVHLH
GGVTPDDSDGYPEAWFSKDFEQTGPYFKREVYHYPNQQRGAILWYHDHAM
ALTRLNVYAGLVGAYIIHDPKEKRLKLPSDEYDVPLLITDRTINEDGSLF
YPSAPENPSPSLPNPSIVPAFCGETILVNGKVWPYLEVEPRKYRFRVINA
SNTRTYNLSLDNGGDFIQIGSDGGLLPRSVKLNSFSLAPAERYDIIIDFT
AYEGESIILANSAGCGGDVNPETDANIMQFRVTKPLAQKDESRKPKYLAS
YPSVQHERIQNIRTLKLAGTQDEYGRPVLLLNNKRWHDPVTETPKVGTTE
IWSIINPTRGTHPIHLHLVSFRVLDRRPFDIARYQESGELSYTGPAVPPP
PSEKGWKDTIQAHAGEVLRIAATFGPYSGRYVWHCHILEHEDYDMMRPMD
ITDP
3D structure
PDB2bhf Dioxygen Reduction by Multi-Copper Oxidases; a Structural Perspective.
ChainA
Resolution2.5 Å
3D
structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]
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 CU1 A H419 C492 H497 H412 C485 H490
BS02 CU1 A H107 H153 H493 H100 H146 H486
BS03 CU1 A H155 H424 H491 H148 H417 H484
BS04 CU1 A H105 H107 H422 H424 H98 H100 H415 H417
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

View graph for
Molecular Function
View graph for
Biological Process
View graph for
Cellular Component
External links
PDB RCSB:2bhf, PDBe:2bhf, PDBj:2bhf
PDBsum2bhf
PubMed16234932
UniProtP07788|COTA_BACSU Laccase (Gene Name=cotA)

[Back to BioLiP]