Structure of PDB 4yfb Chain L

Receptor sequence
>4yfbL (length=574) Species: 1268622 (Acidovorax sp. MR-S7) [Search protein sequence]
SNMYGFGTAATGEGSGVLFGNPHWYWKGPDRFYQAQLTIDGEANVSGVSF
LGLPVIQIGFNDSVAWSHTVSTARRFGFFQLSLVQGEPTSYLRDGVPVKM
KPATITVPSRNADGSVSDVTRTLYHSEFGPLVNLAGLNPALAWSQGTAFA
IRDINGENFRTLRTWMRWNQAKSLDEFIAIQKEEASIPWVNTVAVGRGSA
KAWYADIGAVPNVSPAQTAACTTPFGMAVGQALPNVPFFDGSRSECDWLT
DADSVQKGAVGVSRMPSLQRDDYVGNMNDSYWLANVHAPLTGYPAIFGPA
GTSAQTLRTRMGHTMALERLAGTDGYAGNKATSAVVREMVLGSRVFSAER
FKDEVLDLICTPAQWTVNGAAVDAAQACAVLAAWDNRGRKDSRGSHLWDE
FWSRVPTASLFTVPFSAADPLNTPRGINAAAADALRQAMATAIARVGQSG
YALDAPRGEVLYATRGGTRLPLYGGCGAMGYFTITCSENDITQGGYSMDG
QPNASNSYMQVVSFPASGVQAHTFLTFSLSDDPASPHHGDYTKAYSAGQW
LRVPFTEAEITGNADYRTATVKEL
3D structure
PDB4yfb Bifunctional quorum-quenching and antibiotic-acylase MacQ forms a 170-kDa capsule-shaped molecule containing spacer polypeptides
ChainL
Resolution1.75 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 W24 V70 L137 N138 P139 A228 V229 N503 W24 V70 L137 N138 P139 A228 V229 N503
BS02 PAC L S1 W24 F32 F50 H68 T69 V70 V190 S1 W24 F32 F50 H68 T69 V70 V190
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:4yfb, PDBe:4yfb, PDBj:4yfb
PDBsum4yfb
PubMed28827579
UniProtA0A0A1VBK6

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