Structure of PDB 6dd0 Chain B

Receptor sequence
>6dd0B (length=230) Species: 287 (Pseudomonas aeruginosa) [Search protein sequence]
EYPTVSEIPVGEVRLYQIADGVWSHIATQSFDGAVYPSNGLIVRDGDELL
LIDTAWGAKNTAALLAEIEKQIGLPVTRAVSTHFHDDRVGGVDVLRAAGV
ATYASPSTRRLAEVEGNEIPTHSLEGLSSSGDAVRFGPVELFYPGAAHST
DNLVVYVPSASVLYGGCAIYELSRTSAGNVADADLAEWPTSIERIQQHYP
EAQFVIPGHGLPGGLDLLKHTTNVVKAHTN
3D structure
PDB6dd0 Heteroaryl Phosphonates as Noncovalent Inhibitors of Both Serine- and Metallocarbapenemases.
ChainB
Resolution1.5 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) H116 H118 D120 H196 C221 Y224 N233 H263
Catalytic site (residue number reindexed from 1) H83 H85 D87 H148 C167 Y170 N179 H209
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 H116 H118 H196 H83 H85 H148
BS02 ZN B D120 C221 H263 D87 C167 H209
BS03 P9T B F61 Y67 H118 D120 H196 C221 R228 N233 H263 F31 Y36 H85 D87 H148 C167 R174 N179 H209 MOAD: Ki=3.3uM
Gene Ontology
Molecular Function
GO:0016787 hydrolase activity
GO:0046872 metal ion binding
Biological Process
GO:0017001 antibiotic catabolic process

View graph for
Molecular Function
View graph for
Biological Process
External links
PDB RCSB:6dd0, PDBe:6dd0, PDBj:6dd0
PDBsum6dd0
PubMed31483651
UniProtQ9K2N0

[Back to BioLiP]