Structure of PDB 6m5q Chain A

Receptor sequence
>6m5qA (length=357) Species: 573 (Klebsiella pneumoniae) [Search protein sequence]
HHHANIDESKIKDTVDDLIQPLMQKNNIPGMSVAVTVNGKNYIYNYGLAA
KQPQQPVTENTLFEVGSLSKTFAATLASYAQVSGKLSLDQSVSHYVPELR
GSSFDHVSVLNVGTHTSGLQLFMPEDIKNTTQLMAYLKAWKPADAAGTHR
VFSNIGTGLLGMIAAKSLGVSYEDAIEKTLLPQLGMHHSYLKVPADQMEN
YAWGYNKKDEPVHVNMEILGNEAYGIKTTSSDLLRYVQANMGQLKLDANA
KMQQALTATHTGYFKSGEITQDLMWEQLPYPVSLPNLLTGNKSVATPIVP
PLPPQENVWINKTGSTNGFGAYIAFVPAKKMGIVMLANKNYSIDQRVTVA
YKILSSL
3D structure
PDB6m5q Novel inhibition mechanism of carbapenems on the ACC-1 class C beta-lactamase.
ChainA
Resolution1.3 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) S64 K67 F149 E273 K314 S317
Catalytic site (residue number reindexed from 1) S67 K70 F152 E276 K312 S315
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 IM2 A S64 K67 F149 N151 E273 K314 T315 G316 S317 S67 K70 F152 N154 E276 K312 T313 G314 S315
Gene Ontology
Molecular Function
GO:0000166 nucleotide binding
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

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:6m5q, PDBe:6m5q, PDBj:6m5q
PDBsum6m5q
PubMed32888908
UniProtQ9XB24

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