Structure of PDB 6uah Chain A

Receptor sequence
>6uahA (length=265) Species: 522373 (Stenotrophomonas maltophilia K279a) [Search protein sequence]
APLPQLRAYTVDASWLQPMAPLQVADHTWQIGTEDLTALLVQTAEGAVLL
DGGMPQMAGHLLDNMKLRGVAPQDLRLILLSHAHADHAGPVAELKRRTGA
HVAANAETAVLLARGGSNDLHFGDGITYPPASADRIIMDGEVVTVGGIAF
TAHFMPGHTPGSTAWTWTDTRDGKPVRIAYADSLSAPGYQLKGNPRYPRL
IEDYKRSFATVRALPCDLLLTPHPGASNWNYAVGSKASAEALTCNAYADA
AEKKFDAQLARETAG
3D structure
PDB6uah Crystal Structure of the Metallo-beta-Lactamase L1 from Stenotrophomonas maltophilia in the Complex with Hydrolyzed Meropenem
ChainA
Resolution1.98 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) H105 H107 D109 H110 H181 Y212 H246
Catalytic site (residue number reindexed from 1) H82 H84 D86 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 H105 H107 H181 H82 H84 H158
BS02 ZN A D109 H110 H246 D86 H87 H223
BS03 LMP A Y32 H107 D109 H181 S206 S208 P210 H246 Y9 H84 D86 H158 S183 S185 P187 H223
Gene Ontology
Molecular Function
GO:0008270 zinc ion binding
GO:0008800 beta-lactamase activity
Biological Process
GO:0017001 antibiotic catabolic process

View graph for
Molecular Function
View graph for
Biological Process
External links
PDB RCSB:6uah, PDBe:6uah, PDBj:6uah
PDBsum6uah
PubMed
UniProtB2FTM1

[Back to BioLiP]