Structure of PDB 3wrz Chain B

Receptor sequence
>3wrzB (length=357) Species: 169132 (Chromohalobacter sp. 560) [Search protein sequence]
RQTREVLDPIVASLMEAQQIPGMAIALVRPEGTTISHYGAADRETGTPVD
DDTLFEIGSLSKTLTATLASLAEVEGKLDFDAPVSRYLPELEGSAFDDIS
GLNLGTHTGGGLPLFVPDEVTDRASLMAWYREWQPTEPIGESRTYSNLGI
GLLGLETAASLDGEFVPTMRAKVLAPLGMQDTWYDVPEARMADYAMGEDK
DGQPTRVSPGVLDDEAYGIKTTAADLAKLVRANLHLADVDAELQQAIDAT
RQGHYRVGDMTQALIWEQYSLPVAPETLRAGQGYDMILEPNAAEALEPPQ
SPRDDVWVNKTGSTQGFGGYIVMLPGKHTGLVMLANKNYPNDARVEAAYR
ILSGLGA
3D structure
PDB3wrz Structure of a highly acidic beta-lactamase from the moderate halophile Chromohalobacter sp. 560 and the discovery of a Cs(+)-selective binding site
ChainB
Resolution1.8 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) S65 K68 Y151 E273 K316 S319
Catalytic site (residue number reindexed from 1) S59 K62 Y145 E267 K310 S313
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 CA B D219 D220 D213 D214
BS02 CA B D291 E295 D285 E289
Gene Ontology
Molecular Function
GO:0008800 beta-lactamase activity
GO:0016787 hydrolase activity
GO:0046872 metal ion binding
Biological Process
GO:0017001 antibiotic catabolic process
GO:0046677 response to antibiotic
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:3wrz, PDBe:3wrz, PDBj:3wrz
PDBsum3wrz
PubMed25760604
UniProtQ76LX5

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