Structure of PDB 2fu8 Chain B

Receptor sequence
>2fu8B (length=266) Species: 40324 (Stenotrophomonas maltophilia) [Search protein sequence]
EVPLPQLRAYTVDASWLQPMAPLQIADHTWQIGTEDLTALLVQTPDGAVL
LDGGMPQMASHLLDNMKARGVTPRDLRLILLSHAHADHAGPVAELKRRTG
AKVAANAESAVLLARGGSDDLHFGDGITYPPANADRIVMDGEVITVGGIV
FTAHFMAGHTPGSTAWTWTDTRNGKPVRIAYADSLSAPGYQLQGNPRYPH
LIEDYRRSFATVRALPCDVLLTPHPGASNWDYAAGARAGAKALTCKAYAD
AAEQKFDGQLAKETAG
3D structure
PDB2fu8 Structural insights into the design of inhibitors for the L1 metallo-beta-lactamase from Stenotrophomonas maltophilia.
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) H116 H118 D120 H121 H196 Y229 H263
Catalytic site (residue number reindexed from 1) H83 H85 D87 H88 H159 Y190 H224
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 H116 H118 H196 H83 H85 H159
BS02 ZN B D120 H121 H263 D87 H88 H224
BS03 MCO B Y33 W39 D120 H196 S225 P227 H263 Y10 W16 D87 H159 S186 P188 H224 MOAD: Ki=20uM
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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Cellular Component
External links
PDB RCSB:2fu8, PDBe:2fu8, PDBj:2fu8
PDBsum2fu8
PubMed17999929
UniProtP52700|BLA1_STEMA Metallo-beta-lactamase L1 type 3

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