Structure of PDB 5k1d Chain A

Receptor sequence
>5k1dA (length=359) Species: 548 (Klebsiella aerogenes) [Search protein sequence]
HHGEASPVDPLRPVVDASIQPLLKEHRIPGMAVAVLKDGKAHYFNYGVAN
RESGAGVSEQTLFEIGSVSKTLTATLGAYAVVKGAMQLDDKASRHAPWLK
GSAFDSITMGELATYSAGGLPLQFPEEVDSSEKMRAYYRQWAPVYSPGSH
RQYSNPSIGLFGHLAASSLKQPFAPLMEQTLLPGLGMHHTYVNVPKQAMA
SYAYGYSKEDKPIRVNPGMLADEAYGIKTSSADLLRFVKANIGGVDDKAL
QQAISLTHQGHYSVGGMTQGLGWESYAYPVTEQTLLAGNSAKVILEANPT
AAPRESQVLFNKTGSTNGFGAYVAFVPARGIGIVMLANRNYPIEARIKAA
HAILAQLAG
3D structure
PDB5k1d GMP and IMP Are Competitive Inhibitors of CMY-10, an Extended-Spectrum Class C beta-Lactamase.
ChainA
Resolution1.94 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) S65 K68 M107 E109 F122 Y151 G157 E272 K312 S315
Catalytic site (residue number reindexed from 1) S67 K70 M109 E111 F124 Y153 G159 E274 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 5GP A S65 L120 Q121 Y151 I292 L293 T313 G314 S315 I343 S67 L122 Q123 Y153 I294 L295 T313 G314 S315 I343 MOAD: Ki=20.8uM
PDBbind-CN: -logKd/Ki=4.68,Ki=20.8uM
Gene Ontology
Molecular Function
GO:0000166 nucleotide binding
GO:0008800 beta-lactamase activity
GO:0016787 hydrolase activity
GO:0046872 metal ion binding
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:5k1d, PDBe:5k1d, PDBj:5k1d
PDBsum5k1d
PubMed28242658
UniProtQ99QC1

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