Structure of PDB 5v83 Chain A

Receptor sequence
>5v83A (length=364) Species: 9606,10665 [Search protein sequence]
SQDLENLYFQGSMNIFEMLRIDEGLRLKIYKDTEGYYTIGIGHLLTKSPS
LNAAKSELDKAIGRNTNGVITKDEAEKLFNQDVDAAVRGILRNAKLKPVY
DSLDAVRRAALINMVFQMGETGVAGFTNSLRMLQQKRWDEAAVNLAKSRW
YNQTPNRTKRVITTFRTGTWDAYKNLRKKLEQLYNRYKDPQDENKIGIDG
IQQFCDDLALDPASISVLIIAWKFRAATQCEFSKQEFMDGMTELGCDSIE
KLKAQIPKMEQELKEPGRFKDFYQFTFNFAKNPGLDLEMAIAYWNLVLNG
RFKFLDLWNKFLLEHHKRSIPKDTWNLLLDFSTMIADDMSNYDEEGAWPV
LIDDFVEFARPQIA
3D structure
PDB5v83 Blocking an N-terminal acetylation-dependent protein interaction inhibits an E3 ligase.
ChainA
Resolution2.002 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) E11 D20
Catalytic site (residue number reindexed from 1) E23 D32
Enzyme Commision number 3.2.1.17: lysozyme.
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 8Z7 A I1086 F1089 P1097 A1098 V1102 I1105 A1106 A1111 Q1114 E1116 F1117 F1164 A1180 Y1181 L1184 I201 F204 P212 A213 V217 I220 A221 A226 Q229 E231 F232 F279 A292 Y293 L296 MOAD: ic50=7uM
PDBbind-CN: -logKd/Ki=5.16,IC50=6.91uM
Gene Ontology
Molecular Function
GO:0003796 lysozyme activity
GO:0016798 hydrolase activity, acting on glycosyl bonds
Biological Process
GO:0009253 peptidoglycan catabolic process
GO:0016998 cell wall macromolecule catabolic process
GO:0031640 killing of cells of another organism
GO:0042742 defense response to bacterium
GO:0044659 viral release from host cell by cytolysis
Cellular Component
GO:0030430 host cell cytoplasm

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Cellular Component
External links
PDB RCSB:5v83, PDBe:5v83, PDBj:5v83
PDBsum5v83
PubMed28581483
UniProtP00720|ENLYS_BPT4 Endolysin (Gene Name=E);
Q96GG9|DCNL1_HUMAN DCN1-like protein 1 (Gene Name=DCUN1D1)

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