BioLiP

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

PDB

8gcy Co-crystal structure of CBL-B in complex with N-Aryl isoindolin-1-one inhibitor

Chain

Resolution

1.81 Å

3D
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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)
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

PDB	RCSB:8gcy, PDBe:8gcy, PDBj:8gcy
PDBsum	8gcy
PubMed	38104184
UniProt	Q13191\|CBLB_HUMAN E3 ubiquitin-protein ligase CBL-B (Gene Name=CBLB)