Structure of PDB 4kza Chain A

Receptor sequence

>4kzaA (length=358) Species: 83333 (Escherichia coli K-12)

APQQINDIVHRTITPLIEQQKIPGMAVAVIYQGKPYYFTWGYADIAKKQP
VTQQTLFELGSVSKTFTGVLGGDAIARGEIKLSDPTTKYWPELTAKQWNG
ITLLHLATYTAGGLPLQVPDEVKSSSDLLRFYQNWQPAWAPGTQRLYANS
SIGLFGALAVKPSGLSFEQAMQTRVFQPLKLNHTWINVPPAEEKNYAWGY
REGKAVHVSPGALDAEAYGVKSTIEDMARWVQSNLKPLDINEKTLQQGIQ
LAQSRYWQTGDMYQGLGWEMLDWPVNPDSIINGSDNKIALAARPVKAITP
PTPAVRASWVHKTGATGGFGSYVAFIPEKELGIVMLANKNYPNPARVDAA
WQILNALQ

3D structure

• PDB: 4kza Increasing chemical space coverage by combining empirical and computational fragment screens.
• Chain: A
• Resolution: 1.6 Å

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	NZ9	A	L254 S257 P306	L251 S254 P303	MOAD: Ki=0.2mM PDBbind-CN: -logKd/Ki=3.70,Ki=0.2mM
BS02	NZ9	A	K24 P26 G206 K342	K21 P23 G203 K339	MOAD: Ki=0.2mM PDBbind-CN: -logKd/Ki=3.70,Ki=0.2mM
BS03	NZ9	A	S64 L119 N152 L293 G317 A318 T319	S61 L116 N149 L290 G314 A315 T316	MOAD: Ki=0.2mM PDBbind-CN: -logKd/Ki=3.70,Ki=0.2mM
BS04	NZ9	A	Q120 V211 S212 Y221 T319 G320	Q117 V208 S209 Y218 T316 G317	MOAD: Ki=0.2mM PDBbind-CN: -logKd/Ki=3.70,Ki=0.2mM

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

External links

• PDB: RCSB:4kza, PDBe:4kza, PDBj:4kza
• PDBsum: 4kza
• PubMed: 24807704
• UniProt: P00811|AMPC_ECOLI Beta-lactamase (Gene Name=ampC)