Structure of PDB 6jka Chain A

Receptor sequence
>6jkaA (length=227) Species: 615 (Serratia marcescens) [Search protein sequence]
GPGVGESLPDLKIEKLDEGVYVHTSFEEVNGWGVVPKHGLVVLVNAEAYL
IDTPFTAKDTEKLVTWFVERGYKIKGSISSHFHSDSTGGIEWLNSRSIPT
YASELTNELLKKDGKVQATNSFSGVNYWLVKNKIEVFYPGPGHTPDNVVV
WLPERKILFGGCFIKPYGLGNLGDANIEAWPKSAKLLKSKYGKAKLVVPS
HSEVGDASLLKLTLEQAVKGLNESKKP
3D structure
PDB6jka Identification of the Inhibitory Compounds for Metallo-beta-lactamases and Structural Analysis of the Binding Modes.
ChainA
Resolution2.006 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) H81 H83 D85 H143 C162 K165 N171 H201
Catalytic site (residue number reindexed from 1) H81 H83 D85 H143 C162 K165 N171 H201
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 H81 H83 H143 H81 H83 H143
BS02 ZN A D85 C162 H201 D85 C162 H201
BS03 BS0 A W32 H83 S84 H143 K165 G170 N171 H201 W32 H83 S84 H143 K165 G170 N171 H201
BS04 BS0 A G31 Y167 Q216 G31 Y167 Q216
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

View graph for
Molecular Function

View graph for
Biological Process

View graph for
Cellular Component
External links
PDB RCSB:6jka, PDBe:6jka, PDBj:6jka
PDBsum6jka
PubMed34853284
UniProtP52699|BLAB_SERMA Metallo-beta-lactamase type 2

[Back to BioLiP]