Structure of PDB 6md8 Chain A

Receptor sequence
>6md8A (length=263) Species: 562 (Escherichia coli) [Search protein sequence]
PTSAVQQKLAALEKSSGGRLGVALIDTADNTQVLYRGDERFPMCSTSKVM
AAAAVLKQSETQKQLLNQPVEIKPADLVNYNPIAEKHVNGTMTLAELSAA
ALQYSDNTAMNKLIAQLGGPGGVTAFARAIGDETFRLDRTEPTLNTAIPG
DPRDTTTPRAMAQTLRQLTLGHALGETQRAQLVTWLKGNTTGAASIRAGL
PTSWTVGDKTGSGDYGTTNDIAVIWPQGRAPLVLVTYFTQPQQNAESRRD
VLASAARIIAEGL
3D structure
PDB6md8 Active-Site Druggability of Carbapenemases and Broad-Spectrum Inhibitor Discovery.
ChainA
Resolution1.4 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) S70 K73 S130 E166 K234 S237
Catalytic site (residue number reindexed from 1) S45 K48 S105 E141 K209 S212
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 J84 A N104 Y105 S130 T235 G236 S237 N79 Y80 S105 T210 G211 S212 MOAD: Ki=4200uM
PDBbind-CN: -logKd/Ki=2.38,Ki=4200uM
BS02 J84 A E25 T26 T55 Q56 V57 G289 L290 E1 T2 T31 Q32 V33 G262 L263 MOAD: Ki=4200uM
PDBbind-CN: -logKd/Ki=2.38,Ki=4200uM
Gene Ontology
Molecular Function
GO:0008800 beta-lactamase activity
GO:0016787 hydrolase activity
GO:0046872 metal ion binding
Biological Process
GO:0017001 antibiotic catabolic process
GO:0030655 beta-lactam antibiotic catabolic process
GO:0046677 response to antibiotic

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Molecular Function
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Biological Process
External links
PDB RCSB:6md8, PDBe:6md8, PDBj:6md8
PDBsum6md8
PubMed30942078
UniProtQ9L5C7

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