Structure of PDB 4e6x Chain B

Receptor sequence
>4e6xB (length=301) Species: 217992 (Escherichia coli O6) [Search protein sequence]
ERLSTLIHQRMQEAKVPALSVSVTIKGVRQRFVYGVADVASQKANTLDTV
YELGSMSKAFTGLVVQILIQEGRLRQGDDIITYLPEMRLNYQGKPASLTV
ADFLYHTSGLPFENLLFAPGAKFSYASANYDVLGAVIENVTGKTFTEVIA
ERLTQPLGMSATVAVIVNKASGYKLGFGKPVLHVPAAYIHSTLPDMEIWI
DAWLHRKALPATLREAMSNSWRGNSDVPLAADNRILYASGWFIDQNQGPY
ISHGGQNPNFSSCIALRPDQQIGIVALANMNSNLILQLCADIDNYLRIGK
Y
3D structure
PDB4e6x The NRP peptidase ClbP as a target for the inhibition of genotoxicity, cell proliferation and tumorogenesis mediated by pks-harboring bacteria
ChainB
Resolution2.24 Å
3D
structure
Catalytic site residues are labeled in the 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
Catalytic site (original residue number in PDB) S95 K98 F152 Y186 S188 D192 H327 Q330 N333
Catalytic site (residue number reindexed from 1) S55 K58 F112 Y125 S127 D131 H253 Q256 N259
Enzyme Commision number 3.5.2.6: beta-lactamase.
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 0NG B S95 Y186 F316 H327 G328 S55 Y125 F242 H253 G254
Gene Ontology
Molecular Function
GO:0008800 beta-lactamase activity
Biological Process
GO:0017001 antibiotic catabolic process
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:4e6x, PDBe:4e6x, PDBj:4e6x
PDBsum4e6x
PubMed
UniProtA0A0H2V8D3

[Back to BioLiP]