Structure of PDB 2qjs Chain C

Receptor sequence
>2qjsC (length=248) Species: 40324 (Stenotrophomonas maltophilia) [Search protein sequence]
PMAPLQIADHTWQIGTEDLTALLVQTPDGAVLLDGGMPQMASHLLDNMKA
RGVTPRDLRLILLSHAHANHAGPVAELKRRTGAKVAANAESAVLLARGGS
DDLHFGDGITYPPANADRIVMDGEVITVGGIVFTAHFMAGHTPGSTAWTW
TDTRNGKPVRIAYADSLSAPGYQLQGNPRYPHLIEDYRRSFATVRALPCD
VLLTPHPGASNWDYAAGARAGAKALTCKAYADAAEQKFDGQLAKETAG
3D structure
PDB2qjs Structural Basis for the Role of Asp-120 in Metallo-beta-lactamases
ChainC
Resolution2.25 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) H116 H118 N120 H121 H196 Y228 H263
Catalytic site (residue number reindexed from 1) H65 H67 N69 H70 H141 Y172 H206
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 C H121 H263 H70 H206
BS02 ZN C H116 H118 H196 H65 H67 H141
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:0030655 beta-lactam antibiotic catabolic process
GO:0046677 response to antibiotic
Cellular Component
GO:0042597 periplasmic space

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Biological Process
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Cellular Component
External links
PDB RCSB:2qjs, PDBe:2qjs, PDBj:2qjs
PDBsum2qjs
PubMed17715946
UniProtP52700|BLA1_STEMA Metallo-beta-lactamase L1 type 3

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