Structure of PDB 4u0x Chain B

Receptor sequence
>4u0xB (length=358) Species: 470 (Acinetobacter baumannii) [Search protein sequence]
NTPKDQEIKKLVDQNFKPLLEKYDVPGMAVGVIQNNKKYEMYYGLQSVQD
KKAVNSNTIFELGSVSKLFTATAGGYAKNKGKISFDDTPGKYWKELKNTP
IDQVNLLQLATYTSGNLALQFPDEVQTDQQVLTFFKDWKPKNPIGEYRQY
SNPSIGLFGKVVALSMNKPFDQVLEKTIFPALGLKHSYVNVPKTQMQNYA
FGYNQENQPIRVNPGPLDAPAYGVKSTLPDMLSFIHANLNPQKYPTDIQR
AINETHQGRYQVNTMYQALGWEEFSYPATLQTLLDSNSEQIVMKPNKVTA
ISKEPSVKMYHKTGSTSGFGTYVVFIPKENIGLVMLTNKRIPNEERIKAA
YVVLNAIK
3D structure
PDB4u0x Biochemical and Structural Analysis of Inhibitors Targeting the ADC-7 Cephalosporinase of Acinetobacter baumannii.
ChainB
Resolution2.03 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 Y150 E272 K312 S315
Catalytic site (residue number reindexed from 1) S64 K67 Y150 E272 K312 S315
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 ZXM B S64 Y150 G314 S315 T316 R340 S64 Y150 G314 S315 T316 R340 PDBbind-CN: -logKd/Ki=6.23,Kd=590nM
Gene Ontology
Molecular Function
GO:0008800 beta-lactamase activity
GO:0016787 hydrolase activity
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:4u0x, PDBe:4u0x, PDBj:4u0x
PDBsum4u0x
PubMed25380506
UniProtQ6DRA1

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