Structure of PDB 4de2 Chain B

Receptor sequence
>4de2B (length=261) Species: 562 (Escherichia coli) [Search protein sequence]
SAVQQKLAALEKSSGGRLGVALIDTADNTQVLYRGDERFPMCSTSKVMAA
AAVLKQSETQKQLLNQPVEIKPADLVNYNPIAEKHVNGTMTLAELSAAAL
QYSDNTAMNKLIAQLGGPGGVTAFARAIGDETFRLDRTEPTLNTAIPGDP
RDTTTPRAMAQTLRQLTLGHALGETQRAQLVTWLKGNTTGAASIRAGLPT
SWTAGDKTGSGDYGTTNDIAVIWPQGRAPLVLVTYFTQPQQNAESRRDVL
ASAARIIAEGL
3D structure
PDB4de2 Structure-Based Design of Potent and Ligand-Efficient Inhibitors of CTX-M Class A Beta-Lactamase
ChainB
Resolution1.4 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) S70 K73 S130 E166 K234 S237
Catalytic site (residue number reindexed from 1) S43 K46 S103 E139 K207 S210
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 DN3 B I155 G156 Q192 G196 H197 A198 I128 G129 Q165 G169 H170 A171 MOAD: Ki=76uM
BS02 DN3 B N104 Y105 S130 N132 P167 N170 T235 G236 S237 G238 D240 N77 Y78 S103 N105 P140 N143 T208 G209 S210 G211 D212 MOAD: Ki=76uM
Gene Ontology
Molecular Function
GO:0008800 beta-lactamase activity
GO:0016787 hydrolase activity
Biological Process
GO:0017001 antibiotic catabolic process
GO:0030655 beta-lactam antibiotic catabolic process
GO:0046677 response to antibiotic

View graph for
Molecular Function
View graph for
Biological Process
External links
PDB RCSB:4de2, PDBe:4de2, PDBj:4de2
PDBsum4de2
PubMed22296601
UniProtQ9L5C8

[Back to BioLiP]