Structure of PDB 1kr3 Chain B

Receptor sequence
>1kr3B (length=227) Species: 817 (Bacteroides fragilis) [Search protein sequence]
SVKISDDISITQLSDKVYTYVSLAEIEGWGMVPSNGMIVINNHQAALLDT
PINDAQTEMLVNWVTDSLHAKVTTFIPNHWHGDCIGGLGYLQRKGVQSYA
NQMTIDLAKEKGLPVPEHGFTDSLTVSLDGMPLQCYYLGGGHATDNIVVW
LPTENILFGGCMLKDNQATSIGNISDADVTAWPKTLDKVKAKFPSARYVV
PGHGDYGGTELIEHTKQIVNQYIESTS
3D structure
PDB1kr3 Identification of a series of tricyclic natural products as potent broad-spectrum inhibitors of metallo-beta-lactamases
ChainB
Resolution2.5 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) H99 H101 D103 H162 C181 K184 N193 H223
Catalytic site (residue number reindexed from 1) H79 H81 D83 H142 C161 K164 N173 H203
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 ZN B H99 H101 H162 H79 H81 H142
BS02 ZN B D103 C181 H223 D83 C161 H203
BS03 113 B H162 C181 K184 S190 N193 H223 H142 C161 K164 S170 N173 H203 MOAD: Ki=10uM
Gene Ontology
Molecular Function
GO:0008270 zinc ion binding
GO:0008800 beta-lactamase activity
Biological Process
GO:0017001 antibiotic catabolic process

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Molecular Function
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Biological Process
External links
PDB RCSB:1kr3, PDBe:1kr3, PDBj:1kr3
PDBsum1kr3
PubMed12019104
UniProtP25910|BLAB_BACFG Metallo-beta-lactamase type 2 (Gene Name=ccrA)

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