Structure of PDB 4yf9 Chain L

Receptor sequence
>4yf9L (length=575) Species: 1268622 (Acidovorax sp. MR-S7) [Search protein sequence]
SNMYGFGTAATGEGSGVLFGNPHWYWKGPDRFYQAQLTIDGEANVSGVSF
LGLPVIQIGFNDSVAWSHTVSTARRFGFFQLSLVQGEPTSYLRDGVPVKM
KPATITVPSRNADGSVSDVTRTLYHSEFGPLVNLAGLNPALAWSQGTAFA
IRDINGENFRTLRTWMRWNQAKSLDEFIAIQKEEASIPWVNTVAVGRGSA
KAWYADIGAVPNVSPAQTAACTTPFGMAVGQALPNVPFFDGSRSECDWLT
DADSVQKGAVGVSRMPSLQRDDYVGNMNDSYWLANVHAPLTGYPAIFGPA
GTSAQTLRTRMGHTMALERLAGTDGYAGNKATSAVVREMVLGSRVFSAER
FKDEVLDLICTPAQWTVNGAAVDAAQACAVLAAWDNRGRKDSRGSHLWDE
FWSRVPTASLFTVPFSAADPLNTPRGINAAAADALRQAMATAIARVGQSG
YALDAPRGEVLYATRGGTRLPLYGGCGAMGYFTITCSENDITQGGYSMDG
QPNASNSYMQVVSFPASGVQAHTFLTFSLSDDPASPHHGDYTKAYSAGQW
LRVPFTEAEITGNADYRTATVKELE
3D structure
PDB4yf9 Bifunctional quorum-quenching and antibiotic-acylase MacQ forms a 170-kDa capsule-shaped molecule containing spacer polypeptides
ChainL
Resolution2.6 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) S1 H23 V70 N278 N506
Catalytic site (residue number reindexed from 1) S1 H23 V70 N278 N506
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 peptide L V70 R74 L137 N138 A228 L233 V70 R74 L137 N138 A228 L233
Gene Ontology
Molecular Function
GO:0016787 hydrolase activity
Biological Process
GO:0017000 antibiotic biosynthetic process

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Molecular Function
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Biological Process
External links
PDB RCSB:4yf9, PDBe:4yf9, PDBj:4yf9
PDBsum4yf9
PubMed28827579
UniProtA0A0A1VBK6

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