Structure of PDB 4c1g Chain B

Receptor sequence
>4c1gB (length=217) Species: 615 (Serratia marcescens) [Search protein sequence]
LPDLKIEKLDEGVYVHTSFEEVNGWGVVPKHGLVVLVNAEAYLIDTPFTA
KDTEKLVTWFVERGYKIKGSISSHFHSDSTGGIEWLNSRSIPTYASELTN
ELLKKDGKVQATNSFSGVNYWLVKNKIEVFYPGPGHTPDNVVVWLPERKI
LFGGCFIKPYGLGNLGDANIEAWPKSAKLLKSKYGKAKLVVPSHSEVGDA
SLLKLTLEQAVKGLNES
3D structure
PDB4c1g Structural Basis of Metallo-beta-Lactamase Inhibition by Captopril Stereoisomers.
ChainB
Resolution1.714 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) H95 H97 D99 H157 C176 K179 N185 H215
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 B D99 C176 H215 D78 C155 H194
BS02 ZN B H95 H97 H157 H74 H76 H136
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:4c1g, PDBe:4c1g, PDBj:4c1g
PDBsum4c1g
PubMed26482303
UniProtP52699|BLAB_SERMA Metallo-beta-lactamase type 2

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