Structure of PDB 6m5p Chain A

Receptor sequence
>6m5pA (length=359) Species: 573 (Klebsiella pneumoniae) [Search protein sequence]
HHHANIDESKIKDTVDDLIQPLMQKNNIPGMSVAVTVNGKNYIYNYGLAA
KQPQQPVTENTLFEVGSLSKTFAATLASYAQVSGKLSLDQSVSHYVPELR
GSSFDHVSVLNVGTHTSGLQLFMPEDIKNTTQLMAYLKAWKPADAAGTHR
VFSNIGTGLLGMIAAKSLGVSYEDAIEKTLLPQLGMHHSYLKVPADQMEN
YAWGYNKKDEPVHVNMEILGNEAYGIKTTSSDLLRYVQANMGQLKLANAK
MQQALTATHTGYFKSGEITQDLMWEQLPYPVSLPNLLTGNSVATPIVPPL
PPQENVWINKTGSTNGFGAYIAFVPAKKMGIVMLANKNYSIDQRVTVAYK
ILSSLEGNK
3D structure
PDB6m5p Novel inhibition mechanism of carbapenems on the ACC-1 class C beta-lactamase.
ChainA
Resolution1.25 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 E275 K310 S313
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 MER A S64 K67 L118 F149 N151 E273 N288 N313 K314 T315 G316 S317 S67 K70 L121 F152 N154 E275 N290 N309 K310 T311 G312 S313
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:6m5p, PDBe:6m5p, PDBj:6m5p
PDBsum6m5p
PubMed32888908
UniProtQ9XB24

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