2C2V: CHIP-UBC13-UEV1a complex

Name: PDB 2C2V: Crystal structure of the CHIP-UBC13-UEV1a complex
Published: 2005-11-23
License: https://creativecommons.org/publicdomain/zero/1.0/
Keywords: chaperone

Crystal structure of the CHIP-UBC13-UEV1a complex. Determined by X-ray diffraction at 2.9 Å resolution. Released 23 Nov 2005.

Method: X-ray diffraction
Resolution: 2.9 Å
Organisms: Homo sapiens, Mus musculus
Chains: 12
Atoms: 11,636
Mol. weight: 169.48 kDa
Released: 23 Nov 2005

Explore 2C2V in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

2C2V contains 65 α-helices and 91 β-strands across 12 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 B: 6 helices, 7 β-strands

Element	Residues	Length	Sheet
α-helix	10-21	12
α-helix	23-24	2
β-strand	27-31	5	1
β-strand	38-44	7	1
α-helix	45-46	2
β-strand	55-61	7	1
β-strand	72-75	4	1
β-strand	84	1	2
β-strand	89	1	1
β-strand	90	1	2
α-helix	93-96	4
α-helix	105-115	11
α-helix	128-151	24

Chain C: 5 helices, 9 β-strands

Element	Residues	Length	Sheet
α-helix	40-52	13
β-strand	60-64	5	3
β-strand	74-80	7	3
β-strand	91-97	7	3
α-helix	106-107	2
β-strand	108-111	4	3
β-strand	113	1	4
β-strand	120	1	5
β-strand	126	1	3
β-strand	127	1	5
α-helix	133-136	4
α-helix	144-154	11
α-helix	163-167	5
β-strand	171	1	4

Chain E: 7 helices, 6 β-strands

Element	Residues	Length	Sheet
α-helix	10-21	12
α-helix	23	1
β-strand	24	1	6
β-strand	27-32	6	6
β-strand	35-44	10	6
β-strand	55-61	7	6
α-helix	70-71	2
β-strand	72-75	4	6
β-strand	89	1	6
α-helix	93-95	3
α-helix	105-117	13
α-helix	128-135	8
α-helix	137-151	15

Chain F: 6 helices, 9 β-strands

Element	Residues	Length	Sheet
α-helix	40-53	14
β-strand	60-64	5	7
β-strand	74-80	7	7
β-strand	91-97	7	7
α-helix	106-107	2
β-strand	108-111	4	7
β-strand	113	1	8
β-strand	120	1	9
β-strand	126	1	7
β-strand	127	1	9
α-helix	128	1
α-helix	129-131	3
α-helix	133-136	4
α-helix	144-155	12
β-strand	171	1	8

Chain H: 7 helices, 9 β-strands

Element	Residues	Length	Sheet
α-helix	10-21	12
β-strand	24	1	10
β-strand	27	1	10
β-strand	28-32	5	11
β-strand	35-44	10	11
β-strand	55-61	7	11
α-helix	70-71	2
β-strand	72-75	4	11
β-strand	84	1	12
β-strand	89	1	11
β-strand	90	1	12
α-helix	93-96	4
α-helix	105-117	13
α-helix	128-135	8
α-helix	139-147	9
α-helix	148-152	5

Chain I: 6 helices, 7 β-strands

Element	Residues	Length	Sheet
α-helix	40-53	14
β-strand	61-64	4	13
β-strand	74-80	7	13
β-strand	91-97	7	13
α-helix	106-107	2
β-strand	108-111	4	13
β-strand	120	1	14
β-strand	126	1	13
β-strand	127	1	14
α-helix	128	1
α-helix	133-136	4
α-helix	144-156	13
α-helix	158-161	4

Chain K: 7 helices, 7 β-strands

Element	Residues	Length	Sheet
α-helix	10-21	12
β-strand	27-32	6	15
β-strand	35-44	10	15
α-helix	45-46	2
β-strand	55-61	7	15
α-helix	70-71	2
β-strand	72-75	4	15
β-strand	84	1	16
β-strand	89	1	15
β-strand	90	1	16
α-helix	93-96	4
α-helix	105-117	13
α-helix	128-130	3
α-helix	137-152	16

Chain L: 6 helices, 10 β-strands

Element	Residues	Length	Sheet
α-helix	40-53	14
β-strand	62-64	3	17
β-strand	74-79	6	17
β-strand	92-97	6	17
α-helix	106-107	2
β-strand	108-111	4	17
β-strand	113	1	18
β-strand	117	1	19
β-strand	120	1	19
β-strand	126	1	17
β-strand	127	1	19
α-helix	129-131	3
α-helix	133-136	4
α-helix	144-154	11
α-helix	158-161	4
β-strand	171	1	18

4 more chain groups are not listed. Open the entry in the viewer and use the sequence panel to see them.

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Ubiquitin-conjugating enzyme E2 N	B, E, H, K	protein	154	Homo sapiens	P61088 (AlphaFold model)
Ubiquitin-conjugating enzyme E2 variant 1	C, F, I, L	protein	142	Homo sapiens	Q13404 (AlphaFold model)
STIP1 homology and U box-containing protein 1	S, T, U, V	protein	78	Mus musculus	Q9WUD1 (AlphaFold model)

Sequence of entity 1 (B, E, H, K), FASTA

>2C2V_1 Ubiquitin-conjugating enzyme E2 N (chains B, E, H, K)
AGSAGLPRRIIKETQRLLAEPVPGIKAEPDESNARYFHVVIAGPQDSPFEGGTFKLELFL
PEEYPMAAPKVRFMTKIYHPNVDKLGRICLDILKDKWSPALQIRTVLLSIQALLSAPNPD
DPLANDVAEQWKTNEAQAIETARAWTRLYAMNNI

Sequence of entity 2 (C, F, I, L), FASTA

>2C2V_2 Ubiquitin-conjugating enzyme E2 variant 1 (chains C, F, I, L)
TTGVKVPRNFRLLEELEEGQKGVGDGTVSWGLEDDEDMTLTRWTGMILGPPRTIYENRIY
SLKIECGPKYPEAPPFVRFVTKINMNGVNSSNGVVDPRAISVLAKWQNSYSIKVVLQELR
RLMMSKENMKLPQPPEGQCYSN

Sequence of entity 3 (S, T, U, V), FASTA

>2C2V_3 STIP1 homology and U box-containing protein 1 (chains S, T, U, V)
DIPDYLCGKISFELMREPCITPSGITYDRKDIEEHLQRVGHFNPVTRSPLTQEQLIPNLA
MKEVIDAFISENGWVEDY

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) 20:525-538. DOI 10.1016/j.molcel.2005.09.023 · PubMed

Other PDB entries of the same protein (UniProt P61088 (AlphaFold model), which also has an AlphaFold model), best resolution first:

4ONL 1.35 Å, Crystal structure of human Mms2/Ubc13_D81N, R85S, A122V, N123P
4ONM 1.35 Å, Crystal structure of human Mms2/Ubc13 - NSC697923
5YWR 1.47 Å, Crystal Structure of RING E3 ligase ZNRF1 in complex with Ube2N (Ubc13)
4ONN 1.5 Å, Crystal structure of human Mms2/Ubc13 - BAY 11-7082
9BIV 1.68 Å, Crystal Structure of Ubc13 with a New Active Site Loop Conformation
9LHJ 1.68 Å, UBE2N/UBE2V2 complexed with a covalent inhibitor
4DHI 1.8 Å, Structure of C. elegans OTUB1 bound to human UBC13
4NR3 1.8 Å, Crystal Structure of a human Mms2/Ubc13 L121G mutant
1J7D 1.85 Å, Crystal Structure of hMms2-hUbc13
4NRG 1.95 Å, Crystal Structure of a human Mms2/Ubc13 D118G mutant
6ULH 1.97 Å, Structure of MavC in complex with its substrate in R3 spacegroup
4TKP 2.08 Å, Complex of Ubc13 with the RING domain of the TRIM5alpha retroviral restriction factor

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