Structure of PDB 5ev6 Chain D

Receptor sequence
>5ev6D (length=218) Species: 615 (Serratia marcescens) [Search protein sequence]
LPDLKIEKLDEGVYVHTSFEEVNGWGVVPKHGLVVLVNAEAYLIDTPFTA
KDTEKLVTWFVERGYKIKGSISSHFHSDSTGGIEWLNSRSIPTYASELTN
ELLKKDGKVQATNSFSGVNYWLVKNKIEVFYPGPGHTPDNVVVWLPERKI
LFGGCFIKPYGLGNLGDANIEAWPKSAKLLKSKYGKAKLVVPSHSEVGDA
SLLKLTLEQAVKGLNESK
3D structure
PDB5ev6 Cross-class metallo-beta-lactamase inhibition by bisthiazolidines reveals multiple binding modes.
ChainD
Resolution1.984 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) H77 H79 D81 H139 C158 K161 N167 H197
Catalytic site (residue number reindexed from 1) H74 H76 D78 H136 C155 K158 N164 H194
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 H77 H79 H139 H74 H76 H136
BS02 ZN D D81 C158 H197 D78 C155 H194
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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Cellular Component
External links
PDB RCSB:5ev6, PDBe:5ev6, PDBj:5ev6
PDBsum5ev6
PubMed27303030
UniProtP52699|BLAB_SERMA Metallo-beta-lactamase type 2

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