Structure of PDB 6p5w Chain A

Receptor sequence
>6p5wA (length=370) Species: 9606,10665 [Search protein sequence]
HSQDLENLYFQGSMNIFEMLRIDEGLRLKIYKDTEGYYTIGIGHLLTKSP
SLNAAKSELDKAIGRNTNGVITKDEAEKLFNQDVDAAVRGILRNAKLKPV
YDSLDAVRRAALINMVFQMGETGVAGFTNSLRMLQQKRWDEAAVNLAKSR
WYNQTPNRTKRVITTFRTGTWDAYKNLRKKLEQLYNRYKDPQDENKIGID
GIQQFCDDLALDPASISVLIIAWKFRAATQCEFSKQEFMDGMTELGCDSI
EKLKAQIPKMEQELKEPGRFKDFYQFTFNFAKNPGQKGLDLEMAIAYWNL
VLNGRFKFLDLWNKFLLEHHSIPKDTWNLLLDFSTMIADDMSNYDEEGAW
PVLIDDFVEFARPQIAGTKS
3D structure
PDB6p5w Discovery of Novel Pyrazolo-pyridone DCN1 Inhibitors Controlling Cullin Neddylation.
ChainA
Resolution1.69 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) E24 D33
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 O0A A I1086 Q1087 P1097 V1102 L1103 Q1114 C1115 E1116 F1117 F1164 A1180 Y1181 L1184 I202 Q203 P213 V218 L219 Q230 C231 E232 F233 F280 A296 Y297 L300 MOAD: ic50=5.1uM
PDBbind-CN: -logKd/Ki=5.29,IC50=5.1uM
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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Molecular Function

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Biological Process

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Cellular Component
External links
PDB RCSB:6p5w, PDBe:6p5w, PDBj:6p5w
PDBsum6p5w
PubMed31465221
UniProtD9IEF7;
Q96GG9|DCNL1_HUMAN DCN1-like protein 1 (Gene Name=DCUN1D1)

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