Structure of PDB 6uah Chain A Binding Site BS01
Receptor Information
>6uah Chain A (length=265) Species:
522373
(Stenotrophomonas maltophilia K279a) [
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APLPQLRAYTVDASWLQPMAPLQVADHTWQIGTEDLTALLVQTAEGAVLL
DGGMPQMAGHLLDNMKLRGVAPQDLRLILLSHAHADHAGPVAELKRRTGA
HVAANAETAVLLARGGSNDLHFGDGITYPPASADRIIMDGEVVTVGGIAF
TAHFMPGHTPGSTAWTWTDTRDGKPVRIAYADSLSAPGYQLKGNPRYPRL
IEDYKRSFATVRALPCDLLLTPHPGASNWNYAVGSKASAEALTCNAYADA
AEKKFDAQLARETAG
Ligand information
Ligand ID
ZN
InChI
InChI=1S/Zn/q+2
InChIKey
PTFCDOFLOPIGGS-UHFFFAOYSA-N
SMILES
Software
SMILES
CACTVS 3.341
[Zn++]
ACDLabs 10.04
OpenEye OEToolkits 1.5.0
[Zn+2]
Formula
Zn
Name
ZINC ION
ChEMBL
CHEMBL1236970
DrugBank
DB14532
ZINC
PDB chain
6uah Chain A Residue 301 [
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Receptor-Ligand Complex Structure
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PDB
6uah
Crystal Structure of the Metallo-beta-Lactamase L1 from Stenotrophomonas maltophilia in the Complex with Hydrolyzed Meropenem
Resolution
1.98 Å
Binding residue
(original residue number in PDB)
H105 H107 H181
Binding residue
(residue number reindexed from 1)
H82 H84 H158
Annotation score
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.
Gene Ontology
Molecular Function
GO:0008270
zinc ion binding
GO:0008800
beta-lactamase activity
Biological Process
GO:0017001
antibiotic catabolic process
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Molecular Function
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Biological Process
External links
PDB
RCSB:6uah
,
PDBe:6uah
,
PDBj:6uah
PDBsum
6uah
PubMed
UniProt
B2FTM1
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