Structure of PDB 4tyt Chain A

Receptor sequence
>4tytA (length=218) Species: 1396 (Bacillus cereus) [Search protein sequence]
EKTVIKNTGTISISQLNKNVWVHTELGSAVPSNGLVLNTSKGLVLVDSSW
DDKLTKELIEMVEKKFQKRVTDVIITHAHADRIGGIKTLKERGIKAHSTA
LTAELAKKNGYEEPLGDLQTVTNLKFGNMKVETFYPGKGHTEDNIVVWLP
QYNILVGGCLVKSTSAKDLGNVADAYVNEWSTSIENVLKRYRNINAVVPG
HGEVGDKGLLLHTLDLLK
3D structure
PDB4tyt Rhodanine hydrolysis leads to potent thioenolate mediated metallo-beta-lactamase inhibition.
ChainA
Resolution1.799 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 D120 H179 C198 K201 N210 H240
Catalytic site (residue number reindexed from 1) H77 H79 D81 H140 C159 K162 N171 H201
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 D120 C198 H240 D81 C159 H201
BS02 ZN A H116 H118 H179 H77 H79 H140
BS03 S3C A W89 H118 D120 H179 C198 N210 H240 W50 H79 D81 H140 C159 N171 H201 MOAD: ic50=0.02uM
PDBbind-CN: -logKd/Ki=7.70,IC50=0.02uM
BindingDB: IC50=80nM
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: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:4tyt, PDBe:4tyt, PDBj:4tyt
PDBsum4tyt
PubMed25411887
UniProtP04190|BLA2_BACCE Metallo-beta-lactamase type 2 (Gene Name=blm)

[Back to BioLiP]