Structure of PDB 6skr Chain B

Receptor sequence
>6skrB (length=245) Species: 562 (Escherichia coli) [Search protein sequence]
GSITENTSWNKEFSAEAVNGVFVLCKSSSKSCATNDLARASKEYLPASTF
KIPNAIIGLETGVIKNEHQVFKWDGKPRAMKQWERDLTLRGAIQVSAVPV
FQQIAREVGEVRMQKYLKKFSYGNQNISGGIDKFWLEGQLRISAVNQVEF
LESLYLNKLSASKENQLIVKEALVTEAAPEYLVHSKTGFSGVGTESNPGV
AWWVGWVEKETEVYFFAFNMDIDNESKLPLRKSIPTKIMESEGII
3D structure
PDB6skr Structural insights into the enhanced carbapenemase efficiency of OXA-655 compared to OXA-10.
ChainB
Resolution1.85 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) S67 K70 S115 F120 W154 F208
Catalytic site (residue number reindexed from 1) S48 K51 S96 F101 W135 F189
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 1RG B S67 K70 S115 V117 T206 G207 F208 L247 P248 R250 K251 S48 K51 S96 V98 T187 G188 F189 L228 P229 R231 K232
Gene Ontology
Molecular Function
GO:0008658 penicillin binding
GO:0008800 beta-lactamase activity
Biological Process
GO:0017001 antibiotic catabolic process

View graph for
Molecular Function

View graph for
Biological Process
External links
PDB RCSB:6skr, PDBe:6skr, PDBj:6skr
PDBsum6skr
PubMed32683794
UniProtQ7BNC2

[Back to BioLiP]