Structure of PDB 7z15 Chain I

Receptor sequence
>7z15I (length=253) Species: 562 (Escherichia coli) [Search protein sequence]
QPLLSVNNLTHLYAPGKGFSDVSFDLWPGEVLGIVGESGSGKTTLLKSIS
ARLTPQQGEIHYENRSLYAMSEADRRRLLRTEWGVVHQHPLDGLRRQVSA
GGNIGERLMATGARHYGDIRATAQKWLEEVEIPANRIDDLPTTFSGGMQQ
RLQIARNLVTHPKLVFMDEPTGGLDVSVQARLLDLLRGLVVELNLAVVIV
THDLGVARLLADRLLVMKQGQVVESGLTDRVLDDPHHPYTQLLVSSVLQN
ENL
3D structure
PDB7z15 Structural remodelling of the carbon-phosphorus lyase machinery by a dual ABC ATPase.
ChainI
Resolution1.93 Å
3D
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
Enzyme Commision number ?
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 ADP I Y15 K19 G20 S40 G41 G43 K44 T45 T46 Y13 K17 G18 S38 G39 G41 K42 T43 T44
BS02 MG I T45 Q90 T43 Q88
BS03 ADP I R138 T145 S147 M150 R136 T143 S145 M148
Gene Ontology
Molecular Function
GO:0000166 nucleotide binding
GO:0005515 protein binding
GO:0005524 ATP binding
GO:0016887 ATP hydrolysis activity
Biological Process
GO:0015716 organic phosphonate transport
GO:0015833 peptide transport
GO:0019634 organic phosphonate metabolic process
GO:0019700 organic phosphonate catabolic process
Cellular Component
GO:0061694 alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase complex
GO:1904176 carbon phosphorus lyase complex

View graph for
Molecular Function
View graph for
Biological Process
View graph for
Cellular Component
External links
PDB RCSB:7z15, PDBe:7z15, PDBj:7z15
PDBsum7z15
PubMed36813778
UniProtP16678|PHNK_ECOLI Putative phosphonates utilization ATP-binding protein PhnK (Gene Name=phnK)

[Back to BioLiP]