Structure of PDB 4s2i Chain A

Receptor sequence
>4s2iA (length=259) Species: 573 (Klebsiella pneumoniae) [Search protein sequence]
ADVQQKLAELERQSGGRLGVALINTADNSQILYRADERFAMCSTSKVMAA
AAVLKKSESEPNLLNQRVEIKKSDLVNYNPIAEKHVNGTMSLAELSAAAL
QYSDNVAMNKLIAHVGGPASVTAFARQLGDETFRLDRTEPTLNTAIPGDP
RDTTSPRAMAQTLRNLTLGKALGDSQRAQLVTWMKGNTTGAASIQAGLPA
SWVVGDKTGSGGYGTTNDIAVIWPKDRAPLILVTYFTQPQPKAESRRDVL
ASAAKIVTD
3D structure
PDB4s2i Molecular Mechanism of Avibactam-Mediated beta-Lactamase Inhibition.
ChainA
Resolution1.6 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) S43 K46 S103 E139 K207 S210
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 NXL A C69 S70 N104 S130 N132 N170 T235 G236 S237 C42 S43 N77 S103 N105 N143 T208 G209 S210 PDBbind-CN: -logKd/Ki=9.00,Kd=0.001uM
Gene Ontology
Molecular Function
GO:0008800 beta-lactamase activity
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:4s2i, PDBe:4s2i, PDBj:4s2i
PDBsum4s2i
PubMed27622530
UniProtG3G192

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