Structure of PDB 4kz8 Chain B

Receptor sequence

>4kz8B (length=355) Species: 83333 (Escherichia coli K-12)

QINDIVHRTITPLIEQQKIPGMAVAVIYQGKPYYFTWGYADIAKKQPVTQ
QTLFELGSVSKTFTGVLGGDAIARGEIKLSDPTTKYWPELTAKQWNGITL
LHLATYTAGGLPLQVPDEVKSSSDLLRFYQNWQPAWAPGTQRLYANSSIG
LFGALAVKPSGLSFEQAMQTRVFQPLKLNHTWINVPPAEEKNYAWGYREG
KAVHVSPGALDAEAYGVKSTIEDMARWVQSNLKPLDINEKTLQQGIQLAQ
SRYWQTGDMYQGLGWEMLDWPVNPDSIINGSDNKIALAARPVKAITPPTP
AVRASWVHKTGATGGFGSYVAFIPEKELGIVMLANKNYPNPARVDAAWQI
LNALQ

3D structure

• PDB: 4kz8 Increasing chemical space coverage by combining empirical and computational fragment screens.
• Chain: B
• Resolution: 2.282 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): S58 K61 Y106 A108 V115 Y144 G150 E266 K309 A312
• 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	1U6	B	L254 S257 P306	L248 S251 P300	MOAD: Ki=1.6mM
BS02	1U6	B	I291 R296	I285 R290	MOAD: Ki=1.6mM
BS03	1U6	B	Q120 N152 Y221 A318 T319	Q114 N146 Y215 A312 T313	MOAD: Ki=1.6mM

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:4kz8, PDBe:4kz8, PDBj:4kz8
• PDBsum: 4kz8
• PubMed: 24807704
• UniProt: P00811|AMPC_ECOLI Beta-lactamase (Gene Name=ampC)