Structure of PDB 2gfk Chain A

Receptor sequence

>2gfkA (length=266) Species: 40324 (Stenotrophomonas maltophilia)

EVPLPQLRAYTVDASWLQPMAPLQIADHTWQIGTEDLTALLVQTPDGAVL
LDGGMPQMASHLLDNMKARGVTPRDLRLILLSHAHADHAGPVAELKRRTG
AKVAANAESAVLLARGGSDDLHFGDGITYPPANADRIVMDGEVITVGGIV
FTAHFMAGHTPGSTAWTWTDTRNGKPVRIAYADSLSAPGYQLQGNPRYPH
LIEDYRRSFATVRALPCDVLLTPHPGASNWDYAAGARAGAKALTCKAYAD
AAEQKFDGQLAKETAG

3D structure

• PDB: 2gfk Structural insights into the design of inhibitors for the L1 metallo-beta-lactamase from Stenotrophomonas maltophilia.
• Chain: A
• Resolution: 1.9 Å

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	A	H116 H118 H196	H83 H85 H159
BS02	ZN	A	D120 H121 H263	D87 H88 H224
BS03	VII	A	W39 D120 F156 I162 H196 S225	W16 D87 F123 I127 H159 S186	MOAD: ic50=30uM PDBbind-CN: -logKd/Ki=4.52,IC50=30uM

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

External links

• PDB: RCSB:2gfk, PDBe:2gfk, PDBj:2gfk
• PDBsum: 2gfk
• PubMed: 17999929
• UniProt: P52700|BLA1_STEMA Metallo-beta-lactamase L1 type 3