Structure of PDB 3zni Chain A

Receptor sequence
>3zniA (length=390) Species: 9606 (Homo sapiens) [Search protein sequence]
QAAADRRTVEKTWKLMDKVVRLCQNPKLQLKNSPPYILDILPDTYQHLRL
ILSKYDDNQKLAQLSENEYFKIYIDSLMKKSKRAIRLFKEGKERMYEEQS
QDRRNLTKLSLIFSHMLAEIKAIFPNGQFQGDNFRITKADAAEFWRKFFG
DKTIVPWKVFRQCLHEVHQISSGLEAMALKSTIDLTCNDYISVFEFDIFT
RLFQPWGSILRNWNFLAVTHPGYMAFLTYDEVKARLQKYSTKPGSYIFRL
SCTRLGQWAIGYVTGDGNILQTIPHNKPLFQALIDGSREGFYLYPDGRSY
NPDLTGLCEPTPHDHIKVTQEQFELYCEMGSTFQLCKICAENDKDVKIEP
CGHLMCTSCLTAWQESDGQGCPFCRCEIKGTEPIIVDPFD
3D structure
PDB3zni Essentiality of a Non-Ring Element in Priming Donor Ubiquitin for Catalysis by a Monomeric E3.
ChainA
Resolution2.21 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 peptide A Y266 R286 S288 C289 T290 Q308 T309 P311 F328 Y329 Y229 R249 S251 C252 T253 Q271 T272 P274 F291 Y292
BS02 ZN A C373 C376 C393 C396 C336 C339 C356 C359
BS03 ZN A C388 H390 C408 C411 C351 H353 C371 C374
BS04 CA A D221 T223 N225 Y227 E232 D184 T186 N188 Y190 E195
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:3zni, PDBe:3zni, PDBj:3zni
PDBsum3zni
PubMed23851457
UniProtQ13191|CBLB_HUMAN E3 ubiquitin-protein ligase CBL-B (Gene Name=CBLB)

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