Structure of PDB 1zkj Chain A

Receptor sequence
>1zkjA (length=350) Species: 548 (Klebsiella aerogenes) [Search protein sequence]
DPLRPVVDASIQPLLKEHRIPGMAVAVLKDGKAHYFNYGVANRESGAGVS
EQTLFEIGSVSKTLTATLGAYAVVKGAMQLDDKASRHAPWLKGSAFDSIT
MGELATYSAGGLPLQFPEEVDSSEKMRAYYRQWAPVYSPGSHRQYSNPSI
GLFGHLAASSLKQPFAPLMEQTLLPGLGMHHTYVNVPKQAMASYAYGYSK
EDKPIRVNPGMLADEAYGIKTSSADLLRFVKANIGGVDDKALQQAISLTH
QGHYSVGGMTQGLGWESYAYPVTEQTLLAGNSAKVILEANPTAAPREQVL
FNKTGSTNGFGAYVAFVPARGIGIVMLANRNYPIEARIKAAHAILAQLAG
3D structure
PDB1zkj Structural basis for the extended substrate spectrum of CMY-10, a plasmid-encoded class C beta-lactamase.
ChainA
Resolution1.55 Å
3D
structure
Catalytic site residues are labeled in the structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]
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) S59 K62 M101 E103 F116 Y145 G151 E266 K303 S306
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 ZN A D7 H40 D1 H34
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

View graph for
Molecular Function

View graph for
Biological Process

View graph for
Cellular Component
External links
PDB RCSB:1zkj, PDBe:1zkj, PDBj:1zkj
PDBsum1zkj
PubMed16677302
UniProtQ99QC1

[Back to BioLiP]