Structure of PDB 6tzg Chain D

Receptor sequence
>6tzgD (length=356) Species: 470 (Acinetobacter baumannii) [Search protein sequence]
PKDQEIKKLVDQNFKPLLEKYDVPGMAVGVIQNNKKYEMYYGLQSVQDKK
AVNSNTIFELGSVSKLFTATAGGYAKNKGKISFDDTPGKYWKELKNTPID
QVNLLQLATYTSGNLALQFPDEVQTDQQVLTFFKDWKPKNPIGEYRQYSN
PSIGLFGKVVALSMNKPFDQVLEKTIFPALGLKHSYVNVPKTQMQNYAFG
YNQENQPIRVNPGPLDAPAYGVKSTLPDMLSFIHANLNPQKYPTDIQRAI
NETHQGRYQVNTMYQALGWEEFSYPATLQTLLDSNSEQIVMKPNKVTAIS
KEPSVKMYHKTGSTSGFGTYVVFIPKENIGLVMLTNKRIPNEERIKAAYV
VLNAIK
3D structure
PDB6tzg 1,2,3-Triazolylmethaneboronate: A Structure Activity Relationship Study of a Class of beta-Lactamase Inhibitors againstAcinetobacter baumanniiCephalosporinase.
ChainD
Resolution1.816 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) S62 K65 Y148 E270 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 PKY D S64 Y150 T313 S315 S317 S62 Y148 T311 S313 S315
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:6tzg, PDBe:6tzg, PDBj:6tzg
PDBsum6tzg
PubMed32502340
UniProtQ6DRA1

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