Structure of PDB 1jjt Chain B

Receptor sequence
>1jjtB (length=220) Species: 287 (Pseudomonas aeruginosa) [Search protein sequence]
ESLPDLKIEKLDEGVYVHTSFEEVNGWGVVPKHGLVVLVNAEAYLIDTPF
TAKDTEKLVTWFVERGYKIKGSISSHFHSDSTGGIEWLNSRSIPTYASEL
TNELLKKDGKVQATNSFSGVNYWLVKNKIEVFYPGPGHTPDNVVVWLPER
KILFGGCFIKPYGLGNLGDANIEAWPKSAKLLKSKYGKAKLVVPSHSEVG
DASLLKLTLEQAVKGLNESK
3D structure
PDB1jjt Succinic acids as potent inhibitors of plasmid-borne IMP-1 metallo-beta-lactamase.
ChainB
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) H76 H78 D80 H138 C157 K160 N166 H196
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 H77 H79 H139 H76 H78 H138
BS02 ZN B D81 C158 H197 D80 C157 H196
BS03 ZN B H34 E199 H33 E198
BS04 BDS B W28 H79 S80 D81 H139 C158 K161 G166 N167 H197 W27 H78 S79 D80 H138 C157 K160 G165 N166 H196 MOAD: ic50=0.009uM
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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