Structure of PDB 8gcy Chain A

Receptor sequence
>8gcyA (length=376) Species: 9606 (Homo sapiens) [Search protein sequence]
GQAAADRRTVEKTWALMDAVVRLCQNPKLQLKNSPPYILDILPDTYQHLR
LILSKYDDNQKLAQLSENEYFKIYIDSLMKKSKRAIRLFKEGKERMYEEQ
SQDRRNLTKLSLIFSHMLAEIKAIFPNGQFQGDNFRITKADAAEFWRKFF
GDKTIVPWKVFRQCLHEVHQISSGLEAMALKSTIDLTCNDYISVFEFDIF
TRLFQPWGSILRNWNFLAVTHPGYMAFLTYDEVKARLQKYSTKPGSYIFR
LSCTRLGQWAIGYVTGDGNILQTIPHNKPLFQALIDGSAEGFYLYPDGRS
YNKVTQEQFELYCEMGSTFQLCKICAENDKDVKIEPCGHLMCTSCLTAWQ
ESDGQGCPFCRCEIKGTEPIIVDPFD
3D structure
PDB8gcy Co-crystal structure of CBL-B in complex with N-Aryl isoindolin-1-one inhibitor
ChainA
Resolution1.81 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 2.3.2.27: RING-type E3 ubiquitin transferase.
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 ZN A C373 C376 C393 C396 C322 C325 C342 C345
BS02 ZN A C388 H390 C408 C411 C337 H339 C357 C360
BS03 Z3N A P72 R141 T144 K145 L148 S218 T219 Y260 A262 F263 E268 L287 Y363 M366 P36 R105 T108 K109 L112 S182 T183 Y224 A226 F227 E232 L251 Y312 M315
Gene Ontology
Molecular Function
GO:0001784 phosphotyrosine residue binding
GO:0004842 ubiquitin-protein transferase activity
GO:0005509 calcium ion binding
GO:0046872 metal ion binding
Biological Process
GO:0007166 cell surface receptor signaling pathway
GO:0023051 regulation of signaling

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Molecular Function

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Biological Process
External links
PDB RCSB:8gcy, PDBe:8gcy, PDBj:8gcy
PDBsum8gcy
PubMed38104184
UniProtQ13191|CBLB_HUMAN E3 ubiquitin-protein ligase CBL-B (Gene Name=CBLB)

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