Structure of PDB 2qdt Chain A

Receptor sequence
>2qdtA (length=266) Species: 40324 (Stenotrophomonas maltophilia) [Search protein sequence]
EVPLPQLRAYTVDASWLQPMAPLQIADHTWQIGTEDLTALLVQTPDGAVL
LDGGMPQMASHLLDNMKARGVTPRDLRLILLSHAHADHAGPVAELKRRTG
AKVAANAESAVLLARGGSDDLHFGDGITYPPANADRIVMDGEVITVGGIV
FTAHFMAGHTPGSTAWTWTDTRNGKPVRIAYADSLSAPGYQLQGNPRYPH
LIEDYRRSFATVRALPCDVLLTPHPGASNWDYAAGARAGAKALTCKAYAD
AAEQKFDGQLAKETAG
3D structure
PDB2qdt Structural basis for the broad-spectrum inhibition of metallo-beta-lactamases by thiols.
ChainA
Resolution2.0 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) H84 H86 D88 H89 H160 Y191 H225
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 A H84 H86 H160 H83 H85 H159
BS02 ZN A D88 H89 H225 D87 H88 H224
BS03 I38 A D88 H160 S187 P189 D87 H159 S186 P188 MOAD: Ki=6.5uM
PDBbind-CN: -logKd/Ki=5.19,Ki=6.5uM
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:2qdt, PDBe:2qdt, PDBj:2qdt
PDBsum2qdt
PubMed18563261
UniProtP52700|BLA1_STEMA Metallo-beta-lactamase L1 type 3

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