Structure of PDB 4xxr Chain A

Receptor sequence
>4xxrA (length=262) Species: 562 (Escherichia coli) [Search protein sequence]
TSAVQQKLAALEKSSGGRLGVALIDTADNTQVLYRGDERFPMCSTSKVMA
AAAVLKQSETQKQLLNQPVEIKPADLVNYNPIAEKHVNGTMTLAELSAAA
LQYSDNTAMNKLIAQLGGPGGVTAFARAIGDETFRLDRTAPTLNTAIPGD
PRDTTTPRAMAQTLRQLTLGHALGETQRAQLVTWLKGNTTGAASIRAGLP
TSWTVGDKTGSGDYGTTNDIAVIWPQGRAPLVLVTYFTQPQQNAESRRDV
LASAARIIAEGL
3D structure
PDB4xxr Antibacterial properties and atomic resolution X-ray complex crystal structure of a ruthenocene conjugated beta-lactam antibiotic.
ChainA
Resolution1.18 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) S70 K73 S130 A166 K234 S237
Catalytic site (residue number reindexed from 1) S44 K47 S104 A140 K208 S211
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 JSD A S130 N132 P167 N170 T235 G236 S237 D240 S104 N106 P141 N144 T209 G210 S211 D213
BS02 JSC A K82 I155 H197 A198 K56 I129 H171 A172
BS03 JSE A N54 R184 Q188 R191 N29 R158 Q162 R165
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:0030655 beta-lactam antibiotic catabolic process
GO:0046677 response to antibiotic

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Molecular Function
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Biological Process
External links
PDB RCSB:4xxr, PDBe:4xxr, PDBj:4xxr
PDBsum4xxr
PubMed25753149
UniProtQ9L5C7

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