Structure of PDB 1jjt Chain A

Receptor sequence
>1jjtA (length=220) Species: 287 (Pseudomonas aeruginosa) [Search protein sequence]
SLPDLKIEKLDEGVYVHTSFEEVNGWGVVPKHGLVVLVNAEAYLIDTPFT
AKDTEKLVTWFVERGYKIKGSISSHFHSDSTGGIEWLNSRSIPTYASELT
NELLKKDGKVQATNSFSGVNYWLVKNKIEVFYPGPGHTPDNVVVWLPERK
ILFGGCFIKPYGLGNLGDANIEAWPKSAKLLKSKYGKAKLVVPSHSEVGD
ASLLKLTLEQAVKGLNESKK
3D structure
PDB1jjt Succinic acids as potent inhibitors of plasmid-borne IMP-1 metallo-beta-lactamase.
ChainA
Resolution1.8 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) H77 H79 D81 H139 C158 K161 N167 H197
Catalytic site (residue number reindexed from 1) H75 H77 D79 H137 C156 K159 N165 H195
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 A H77 H79 H139 H75 H77 H137
BS02 ZN A D81 C158 H197 D79 C156 H195
BS03 ZN A H34 E199 H32 E197
BS04 BDS A V25 W28 F51 H79 S80 D81 H139 C158 K161 G166 N167 H197 V23 W26 F49 H77 S78 D79 H137 C156 K159 G164 N165 H195 MOAD: ic50=0.009uM
PDBbind-CN: -logKd/Ki=8.05,IC50=9nM
Gene Ontology
Molecular Function
GO:0008270 zinc ion binding
GO:0008800 beta-lactamase activity
GO:0016787 hydrolase activity
GO:0046872 metal ion binding
Biological Process
GO:0017001 antibiotic catabolic process
GO:0046677 response to antibiotic
Cellular Component
GO:0042597 periplasmic space

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Molecular Function
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Cellular Component
External links
PDB RCSB:1jjt, PDBe:1jjt, PDBj:1jjt
PDBsum1jjt
PubMed11390410
UniProtQ79MP6

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