Structure of PDB 2qin Chain A

Receptor sequence
>2qinA (length=263) Species: 40324 (Stenotrophomonas maltophilia) [Search protein sequence]
VPLPQLRAYTVDASWLQPMAPLQIADHTWQIGTEDLTALLVQTPDGAVLL
DGGMPQMASHLLDNMKARGVTPRDLRLILLSHAHACHAGPVAELKRRTGA
KVAANAESAVLLARGGSDDLHFGDGITYPPANADRIVMDGEVITVGGIVF
TAHFMAGHTPGSTAWTWTDTRNGKPVRIAYADSLSAPGYQLQGNPRYPHL
IEDYRRSFATVRALPCDVLLTPHPGASNWDYAAGARAGAKALTCKAYADA
AEQKFDGQLAKET
3D structure
PDB2qin Structural Basis for the Role of Asp-120 in Metallo-beta-lactamases.
ChainA
Resolution1.76 Å
3D
structure
Catalytic site residues are labeled in the structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]
Enzymatic activity
Catalytic site (original residue number in PDB) H116 H118 C120 H121 H196 Y228 H263
Catalytic site (residue number reindexed from 1) H82 H84 C86 H87 H158 Y189 H223
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 C120 H121 H263 C86 H87 H223
BS02 ZN A H116 H118 H196 H82 H84 H158
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

View graph for
Molecular Function
View graph for
Biological Process
View graph for
Cellular Component
External links
PDB RCSB:2qin, PDBe:2qin, PDBj:2qin
PDBsum2qin
PubMed17715946
UniProtP52700|BLA1_STEMA Metallo-beta-lactamase L1 type 3

[Back to BioLiP]