Structure of PDB 7a63 Chain A

Receptor sequence
>7a63A (length=266) Species: 40324 (Stenotrophomonas maltophilia) [Search protein sequence]
EVPLPQLRAYTVDASWLQPMAPLQIADHTWQIGTEDLTALLVQTPDGAVL
LDGGMPQMASHLLDNMKARGVTPRDLRLILLSHAHADHAGPVAELKRRTG
AKVAANAESAVLLARGGSDDLHFGDGITYPPANADRIVMDGEVITVGGIV
FTAHFMAGHTPGSTAWTWTDTRNGKPVRIAYADSLSAPGYQLQGNPRYPH
LIEDYRRSFATVRALPCDVLLTPHPGASNWDYAAGARAGAKALTCKAYAD
AAEQKFDGQLAKETAG
3D structure
PDB7a63 Faropenem reacts with serine and metallo-beta-lactamases to give multiple products.
ChainA
Resolution1.57 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 R3N A Y11 W17 D88 F124 H160 S185 S187 H225 Y10 W16 D87 F123 H159 S184 S186 H224
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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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:7a63, PDBe:7a63, PDBj:7a63
PDBsum7a63
PubMed33618159
UniProtP52700|BLA1_STEMA Metallo-beta-lactamase L1 type 3

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