Structure of PDB 5gzw Chain B

Receptor sequence
>5gzwB (length=348) Species: 562 (Escherichia coli) [Search protein sequence]
INDIVHRTITPLIEQQKIPGMAVAVIYQGKPYYFTWGYADIAKKQPVTQQ
TLFELGSVSKTFTGVLGGDAIARGEIKLSDPATKYWPELTAKQWNGITLL
HLATYTAGGLPLQVPDEVKSSSDLLRFYQNWQPAWAPGTQRLYANSSIGL
FGALAVKPSGLSFEQAMQTRVFQPLKLNHTWINVPPPEEKNYAWGYREGK
AVHVSPGALDAEAYGVKSTIEDMARWVRSNMNPRDINDKTLQQGIQLAQS
RYWQTGDMYQGLGWEMLDWPVNPDSIINGSAAHPVKAITPPTPAVRASWV
HKTGATGGFGSYVAFIPEKELGIVMLANKNYPNPARVAAAWQILNALQ
3D structure
PDB5gzw Structural and mechanistic insights into the inhibition of class C beta-lactamases through the adenylylation of the nucleophilic serine.
ChainB
Resolution1.489 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) S64 K67 Y112 A114 V121 Y150 G156 E272 K317 A320
Catalytic site (residue number reindexed from 1) S57 K60 Y105 A107 V114 Y143 G149 E265 K302 A305
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 AMP B S64 Q120 Y150 N152 Y221 G319 A320 T321 S57 Q113 Y143 N145 Y214 G304 A305 T306
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

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:5gzw, PDBe:5gzw, PDBj:5gzw
PDBsum5gzw
PubMed27999057
UniProtA0A076YIY5

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