Structure of PDB 5zlk Chain A

Receptor sequence
>5zlkA (length=506) Species: 224308 (Bacillus subtilis subsp. subtilis str. 168) [Search protein sequence]
TLEKFVDALPIPDTLKPVQQSKEKTYYEVTMEECTHQLHRDLPPTRLWGY
NGLFPGPTIEVKRNENVYVKWMNNLPSTHFLPIDHTIHHSEEPEVKTVVH
LHGGVTPDDSDGYPEAWFSKDFEQTGPYFKREVYHYPNQQRGAILWYHDH
AMALTRLNVYAGLVGAYIIHDPKEKRLKLPSDEYDVPLLITDRTINEDGS
LFYPSAPENPSPSLPNPSIVPAFCGETILVNGKVWPYLEVEPRKYRFRVI
NASNTRTYNLSLDNGGDFIQIGSDGGLLPRSVKLNSFSLAPAERYDIIID
FTAYEGESIILANSAGCGGDVNPETDANIMQFRVTKPLAQKDESRKPKYL
ASYPSVQHERIQNIRTLKLAGTQDEYGRPVLLLNNKRWHDPVTETPKVGT
TEIWSIINPTRGTHPIHLHLVSFRVLDRRPFDIARYQESGELSYTGPAVP
PPPSEKGWKDTIQAHAGEVLRIAATFGPYSGRYVWHCAILEHEDYDMMRP
MDITDP
3D structure
PDB5zlk Structural Insight into the Allosteric Coupling of Cu1 Site and Trinuclear Cu Cluster in CotA Laccase.
ChainA
Resolution2.6 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 CU A H419 C492 H497 H414 C487 H492
BS02 CU A H105 H107 H422 H424 H100 H102 H417 H419
BS03 CU A H155 H424 H491 H150 H419 H486
BS04 CU A H107 H153 H102 H148
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:5zlk, PDBe:5zlk, PDBj:5zlk
PDBsum5zlk
PubMed29722464
UniProtP07788|COTA_BACSU Laccase (Gene Name=cotA)

[Back to BioLiP]