2C2L: CHIP U-box E3 ubiquitin ligase

Name: PDB 2C2L: Crystal structure of the CHIP U-box E3 ubiquitin ligase
Published: 2005-11-23
License: https://creativecommons.org/publicdomain/zero/1.0/
Keywords: chaperone

Crystal structure of the CHIP U-box E3 ubiquitin ligase. Determined by X-ray diffraction at 3.3 Å resolution. Released 23 Nov 2005.

Method: X-ray diffraction
Resolution: 3.3 Å
Organisms: MUS MUSCULUS, HOMO SAPIENS
Chains: 8
Atoms: 9,521
Mol. weight: 136.15 kDa
Ligands: NI
Released: 23 Nov 2005

Explore 2C2L in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

2C2L contains 58 α-helices and 24 β-strands across 4 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: 14 helices, 5 β-strands

Element	Residues	Length	Sheet
α-helix	27-39	13
α-helix	43-56	14
α-helix	61-73	13
α-helix	77-87	11
α-helix	95-107	13
α-helix	111-127	17
α-helix	135-153	19
α-helix	161-178	18
α-helix	183-185	3
α-helix	191-194	4
α-helix	196-218	23
β-strand	233	1	1
β-strand	240	1	1
β-strand	244-246	3	2
β-strand	252-254	3	2
α-helix	257-264	8
α-helix	278-280	3
β-strand	282-283	2	2
α-helix	285-295	11

Chains B and D: 15 helices, 7 β-strands

Element	Residues	Length	Sheet
α-helix	27-30	4
α-helix	32-39	8
α-helix	43-56	14
α-helix	61-71	11
α-helix	77-90	14
α-helix	95-104	10
α-helix	111-127	17
α-helix	136-175	40
α-helix	181-184	4
α-helix	192-224	33
α-helix	230-232	3
β-strand	233	1	3
β-strand	240	1	3
β-strand	244-246	3	4
β-strand	252-254	3	4
α-helix	257-262	6
β-strand	268	1	5
β-strand	275	1	5
α-helix	278-280	3
β-strand	282-283	2	4
α-helix	285-296	12
α-helix	299-301	3

Chain C: 14 helices, 5 β-strands

Element	Residues	Length	Sheet
α-helix	27-39	13
α-helix	43-56	14
α-helix	61-73	13
α-helix	77-87	11
α-helix	95-107	13
α-helix	111-127	17
α-helix	135-153	19
α-helix	161-178	18
α-helix	183-185	3
α-helix	191-194	4
α-helix	196-218	23
β-strand	233	1	6
β-strand	240	1	6
β-strand	244-246	3	7
β-strand	252-254	3	7
α-helix	257-260	4
α-helix	278-280	3
β-strand	282-283	2	7
α-helix	285-295	11

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Carboxy terminus of HSP70-interacting protein	A, B, C, D	protein	281	MUS MUSCULUS	Q9WUD1 (AlphaFold model)
HSP90	E, F, G, H	protein	9	HOMO SAPIENS	P07900 (AlphaFold model)

Sequence of entity 1 (A, B, C, D), FASTA

>2C2L_1 CARBOXY TERMINUS OF HSP70-INTERACTING PROTEIN (chains A, B, C, D)
SPSAQELKEQGNRLFVGRKYPEAAACYGRAITRNPLVAVYYTNRALCYLKMQQPEQALAD
CRRALELDGQSVKAHFFLGQCQLEMESYDEAIANLQRAYSLAKEQRLNFGDDIPSALRIA
KKKRWNSIEERRIHQESELHSYLTRLIAAERERELEECQRNHEGHEDDGHIRAQQACIEA
KHDKYMADMDELFSQVDEKRKKRDIPDYLCGKISFELMREPCITPSGITYDRKDIEEHLQ
RVGHFNPVTRSPLTQEQLIPNLAMKEVIDAFISENGWVEDY

Sequence of entity 2 (E, F, G, H), FASTA

>2C2L_2 HSP90 (chains E, F, G, H)
DTSRMEEVD

Ligands and cofactors

ID	Name	Formula	Copies
NI	Nickel (II) ion	Ni	4

Water and common crystallization additives (SO4) are not listed.

Primary citation

Chaperoned Ubiquitylation-Crystal Structures of the Chip U Box E3 Ubiquitin Ligase and a Chip-Ubc13-Uev1A Complex. Zhang, M., Windheim, M., Roe, S.M. et al. Mol Cell (2005) 20:525. DOI 10.1016/J.MOLCEL.2005.09.023 · PubMed

Other PDB entries of the same protein (UniProt Q9WUD1 (AlphaFold model), which also has an AlphaFold model), best resolution first:

3Q4A 1.54 Å, Crystal structure of the TPR domain of CHIP complexed with phosphorylated Smad1 peptide
3Q49 1.54 Å, Crystal structure of the TPR domain of CHIP complexed with Hsp70-C peptide
3Q47 1.71 Å, Crystal structure of TPR domain of CHIP complexed with pseudophosphorylated Smad1 peptide
2C2V 2.9 Å, Crystal structure of the CHIP-UBC13-UEV1a complex

Browse structure collections

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