Structure of PDB 4bp0 Chain D

Receptor sequence
>4bp0D (length=244) Species: 287 (Pseudomonas aeruginosa) [Search protein sequence]
SDHVDLPYNLTATKIDSDVFVVTDRDFYSSNVLVAKMLDGTVVIVSSPFE
NLGTQTLMDWVAKTMKPKKVVAINTHFHLDGTGGNEIYKKMGAETWSSDL
TKQLRLEENKKDRIKAAEFYKNEDLKRRILSSHPVPADNVFDLKQGKVFS
FSNELVEVSFPGPAHSPDNVVVYFPKKKLLFGGCMIKPKELGYLGDANVK
AWPDSARRLKKFDAKIVIPGHGEWGGPEMVNKTIKVAEKAVGEM
3D structure
PDB4bp0 Studying the active-site loop movement of the Sao Paolo metallo-beta-lactamase-1
ChainD
Resolution2.24 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) H108 H110 D112 H197 C216 K219 Y228 H258
Catalytic site (residue number reindexed from 1) H76 H78 D80 H165 C184 K187 Y193 H221
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 D H108 H110 H197 H76 H78 H165
BS02 ZN D D112 C216 H258 D80 C184 H221
Gene Ontology
Molecular Function
GO:0008270 zinc ion 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:0042597 periplasmic space

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:4bp0, PDBe:4bp0, PDBj:4bp0
PDBsum4bp0
PubMed25717359
UniProtQ8G9Q0

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