Structure of PDB 4kzb Chain B

Receptor sequence
>4kzbB (length=358) Species: 83333 (Escherichia coli K-12) [Search protein sequence]
APQQINDIVHRTITPLIEQQKIPGMAVAVIYQGKPYYFTWGYADIAKKQP
VTQQTLFELGSVSKTFTGVLGGDAIARGEIKLSDPTTKYWPELTAKQWNG
ITLLHLATYTAGGLPLQVPDEVKSSSDLLRFYQNWQPAWAPGTQRLYANS
SIGLFGALAVKPSGLSFEQAMQTRVFQPLKLNHTWINVPPAEEKNYAWGY
REGKAVHVSPGALDAEAYGVKSTIEDMARWVQSNLKPLDINEKTLQQGIQ
LAQSRYWQTGDMYQGLGWEMLDWPVNPDSIINGSDNKIALAARPVKAITP
PTPAVRASWVHKTGATGGFGSYVAFIPEKELGIVMLANKNYPNPARVDAA
WQILNALQ
3D structure
PDB4kzb Increasing chemical space coverage by combining empirical and computational fragment screens.
ChainB
Resolution1.37 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) S64 K67 Y112 A114 V121 Y150 G156 E272 K315 A318
Catalytic site (residue number reindexed from 1) S61 K64 Y109 A111 V118 Y147 G153 E269 K312 A315
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 NZ2 B S64 N152 Y221 G317 A318 T319 N343 S61 N149 Y218 G314 A315 T316 N340 MOAD: Ki=1.3mM
BS02 NZ3 B L238 P240 L241 A307 P330 L235 P237 L238 A304 P327 MOAD: Ki=1.3mM
BS03 NZ2 B Q120 V211 S212 Y221 T319 G320 Q117 V208 S209 Y218 T316 G317 MOAD: Ki=1.3mM
Gene Ontology
Molecular Function
GO:0008800 beta-lactamase activity
GO:0016787 hydrolase activity
Biological Process
GO:0017001 antibiotic catabolic process
GO:0046677 response to antibiotic
Cellular Component
GO:0030288 outer membrane-bounded periplasmic space
GO:0042597 periplasmic space

View graph for
Molecular Function
View graph for
Biological Process
View graph for
Cellular Component
External links
PDB RCSB:4kzb, PDBe:4kzb, PDBj:4kzb
PDBsum4kzb
PubMed24807704
UniProtP00811|AMPC_ECOLI Beta-lactamase (Gene Name=ampC)

[Back to BioLiP]