Structure of PDB 6b6a Chain D

Receptor sequence

>6b6aD (length=265) Species: 83332 (Mycobacterium tuberculosis H37Rv)

DLADRFAELERRYDARLGVYVPATGTTAAIEYRADERFAFCSTFKAPLVA
AVLHQNPLTHLDKLITYTSDDIRSISPVAQQHVQTGMTIGQLCDAAIRYS
DGTAANLLLADLGGPGGGTAAFTGYLRSLGDTVSRLDAEEPELNRDPPGD
ERDTTTPHAIALVLQQLVLGNALPPDKRALLTDWMARNTTGAKRIRAGFP
ADWKVIDKTGTGDYGRANDIAVVWSPTGVPYVVAVMSDRAGGGYDAEPRE
ALLAEAATCVAGVLA

3D structure

• PDB: 6b6a Enzyme intermediates captured "on the fly" by mix-and-inject serial crystallography.
• Chain: D
• Resolution: 2.298 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): S70 K73 S128 E168 K236 T239
• Catalytic site (residue number reindexed from 1): S42 K45 S100 E140 K208 T211
• 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	9F2	D	I103 P105 T217	I75 P77 T189
BS02	9F2	D	S70 S128 P169 N172 T218 T237 G238 T239 G240	S42 S100 P141 N144 T190 T209 G210 T211 G212
BS03	FZS	D	C69 S70 S128 P169 N172 T237 G238 T239 G240	C41 S42 S100 P141 N144 T209 G210 T211 G212

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

Cellular Component

• GO:0005576 extracellular region
• GO:0005886 plasma membrane
• GO:0042597 periplasmic space

External links

• PDB: RCSB:6b6a, PDBe:6b6a, PDBj:6b6a
• PDBsum: 6b6a
• PubMed: 29848358
• UniProt: P9WKD3|BLAC_MYCTU Beta-lactamase (Gene Name=blaC)