4A49: PhosphoTyr371-c-Cbl-UbcH5B complex

Structure of phosphoTyr371-c-Cbl-UbcH5B complex. Determined by X-ray diffraction at 2.21 Å resolution. Released 25 Jan 2012.

Method: X-ray diffraction
Resolution: 2.21 Å
Organism: Homo sapiens
Chains: 2
Atoms: 1,955
Mol. weight: 26.43 kDa
Ligands: ZN
Released: 25 Jan 2012

Explore 4A49 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

4A49 contains 11 α-helices and 15 β-strands across 2 chains. Residue ranges use author residue numbering, as in the PDB file, from PDBe. To see them in 3D, choose the Cartoon representation with Secondary structure coloring: helices, sheets and coils get different colors.

Chain A: 3 helices, 7 β-strands

Element	Residues	Length	Sheet
β-strand	360-362	3	1
α-helix	365-373	9
β-strand	380	1	2
β-strand	388	1	2
α-helix	389	1
β-strand	391-394	4	3
β-strand	399-400	2	3
α-helix	402-410	9
β-strand	425-428	4	3
β-strand	430-432	3	1

Chain B: 8 helices, 8 β-strands

Element	Residues	Length	Sheet
α-helix	3-15	13
α-helix	17-18	2
β-strand	21-26	6	4
β-strand	29-38	10	4
α-helix	39-40	2
β-strand	49-55	7	4
α-helix	64-65	2
β-strand	66-69	4	4
β-strand	75	1	5
β-strand	78	1	5
β-strand	83	1	4
β-strand	84	1	5
α-helix	87-89	3
α-helix	99-111	13
α-helix	121-129	9
α-helix	131-145	15

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
E3 ubiquitin-protein ligase CBL	A	protein	84	Homo sapiens	P22681 (AlphaFold model)
Ubiquitin-conjugating enzyme E2 D2	B	protein	147	Homo sapiens	P62837 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>4A49_1 E3 ubiquitin-protein ligase CBL (chains A)
GSEPTPQDHIKVTQEQFELYCEMGSTFQLCKICAENDKDVKIEPCGHLMCTSCLTSWQES
EGQGCPFCRCEIKGTEPIVVDPFD

Sequence of entity 2 (B), FASTA

>4A49_2 Ubiquitin-conjugating enzyme E2 D2 (chains B)
MALKRIHKELNDLARDPPAQCSAGPVGDDMFHWQATIMGPNDSPYQGGVFFLTIHFPTDY
PFKPPKVAFTTRIYHPNINSNGSICLDILRSQWSPALTISKVLLSICSLLCDPNPDDPLV
PEIARIYKTDREKYNRIAREWTQKYAM

Ligands and cofactors

ID	Name	Formula	Copies
ZN	Zinc ion	Zn	2

Water and common crystallization additives (K) are not listed.

Primary citation

Structural basis for autoinhibition and phosphorylation-dependent activation of c-Cbl. Dou, H., Buetow, L., Hock, A. et al. Nat Struct Mol Biol (2012) 19:184-192. DOI 10.1038/nsmb.2231 · PubMed

Other PDB entries of the same protein (UniProt P22681 (AlphaFold model), which also has an AlphaFold model), best resolution first:

3BUX 1.35 Å, Crystal structure of c-Cbl-TKB domain complexed with its binding motif in c-Met
3BUW 1.45 Å, Crystal structure of c-Cbl-TKB domain complexed with its binding motif in Syk
7SIY 1.48 Å, cCBL TKB domain in complex with pZAP70 peptide
5HKY 1.8 Å, Crystal structure of c-Cbl TKBD domain in complex with SPRY2 peptide (36-60, pY55)…
5HKZ 1.8 Å, Crystal Structure of c-Cbl TKBD in complex with SPRY2 peptide (36-60, pY55) Refined to…
5HKX 1.85 Å, Crystal Structure of c-Cbl TKBD-RING domains (Y371E mutant) Refined to 1.85 A Resolution
3PLF 1.92 Å, Reverse Binding Mode of MetRD peptide complexed with c-Cbl TKB domain
2Y1N 2.0 Å, Structure of c-Cbl-ZAP-70 peptide complex
3BUM 2.0 Å, Crystal structure of c-Cbl-TKB domain complexed with its binding motif in Sprouty2
3BUN 2.0 Å, Crystal structure of c-Cbl-TKB domain complexed with its binding motif in Sprouty4
9ERZ 2.02 Å, Structure of CBL-TKBD bound to Ubiquitin-fused CBLock peptide
1YVH 2.05 Å, Crystal Structure of the c-Cbl TKB Domain in Complex with the APS pTyr-618 Phosphopeptide

Browse structure collections

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