1S1Q: TSG101(UEV) domain

TSG101(UEV) domain in complex with Ubiquitin. Determined by X-ray diffraction at 2.0 Å resolution. Released 4 May 2004.

Method: X-ray diffraction
Resolution: 2.0 Å
Organism: Homo sapiens
Chains: 4
Atoms: 3,821
Mol. weight: 51.74 kDa
Ligands: CU
Released: 4 May 2004

Explore 1S1Q in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

1S1Q contains 20 α-helices and 32 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: 6 helices, 9 β-strands

Element	Residues	Length	Sheet
α-helix	5-11	7
α-helix	18-31	14
β-strand	35-43	9	1
β-strand	49-63	15	1
β-strand	66-76	11	1
α-helix	77	1
α-helix	84-85	2
β-strand	86-89	4	1
β-strand	96-97	2	2
β-strand	103	1	3
β-strand	108	1	1
β-strand	109	1	3
α-helix	112-115	4
α-helix	124-137	14
β-strand	141-142	2	2

Chain B: 3 helices, 7 β-strands

Element	Residues	Length	Sheet
β-strand	2-6	5	4
β-strand	13-16	4	4
β-strand	22	1	5
α-helix	23-34	12
α-helix	38-40	3
β-strand	41-45	5	4
β-strand	48-49	2	4
β-strand	55	1	5
α-helix	57-59	3
β-strand	66-71	6	4

Chain C: 6 helices, 9 β-strands

Element	Residues	Length	Sheet
α-helix	5-11	7
α-helix	18-31	14
β-strand	35-43	9	6
β-strand	49-63	15	6
β-strand	66-76	11	6
α-helix	77	1
α-helix	84-85	2
β-strand	86-89	4	6
β-strand	97	1	7
β-strand	103	1	8
β-strand	108	1	6
β-strand	109	1	8
α-helix	112-115	4
α-helix	124-137	14
β-strand	141	1	7

Chain D: 5 helices, 7 β-strands

Element	Residues	Length	Sheet
β-strand	2-6	5	9
α-helix	11-12	2
β-strand	13-16	4	9
β-strand	22	1	10
α-helix	23-34	12
α-helix	38-40	3
β-strand	41-45	5	9
β-strand	48-49	2	9
α-helix	50-51	2
β-strand	55	1	10
α-helix	57-59	3
β-strand	66-71	6	9

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Tumor susceptibility gene 101 protein	A, C	protein	145	Homo sapiens	Q99816 (AlphaFold model)
ubiquitin	B, D	protein	76	Homo sapiens	P0CG48 (AlphaFold model)

Sequence of entity 1 (A, C), FASTA

>1S1Q_1 Tumor susceptibility gene 101 protein (chains A, C)
MAVSESQLKKMVSKYKYRDLTVRETVNVITLYKDLKPVLDSYVFNDGSSRELMNLTGTIP
VPYRGNTYNIPICLWLLDTYPYNPPICFVKPTSSMTIKTGKHVDANGKIYLPYLHEWKHP
QSDLLGLIQVMIVVFGDEPPVFSRP

Sequence of entity 2 (B, D), FASTA

>1S1Q_2 ubiquitin (chains B, D)
MQIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPDQQRLIFAGKQLEDGRTLSDYN
IQKESTLHLVLRLRGG

Ligands and cofactors

ID	Name	Formula	Copies
CU	Copper (II) ion	Cu	4

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

Primary citation

Ubiquitin recognition by the human TSG101 protein. Sundquist, W.I., Schubert, H.L., Kelly, B.N. et al. Mol Cell (2004) 13:783-789. DOI 10.1016/S1097-2765(04)00129-7 · PubMed

Other PDB entries of the same protein (UniProt Q99816 (AlphaFold model), which also has an AlphaFold model), best resolution first:

7NLC 1.4 Å, Crystallographic structure of human Tsg101 UEV domain in complex with a HEV ORF3 peptide
3OBQ 1.4 Å, Crystal Structure of the Tsg101 UEV domain in complex with a human HRS PSAP peptide
3OBS 1.5 Å, Crystal structure of Tsg101 UEV domain
3OBU 1.6 Å, Crystal structure of the Tsg101 UEV domain in complex with a HIV-1 PTAP peptide
3OBX 1.6 Å, Crystal structure of the Tsg101 UEV domain in complex with a HIV-1 Gag P7A mutant peptide
3P9G 1.8 Å, Crystal structure of the TSG101 UEV domain in complex with FA459 peptide
3P9H 1.8 Å, Crystal structure of the TSG101 UEV domain in complex with FA258 peptide
4YC1 2.0 Å, Structure of the human TSG101-UEV domain in the P321 space group
6VME 2.19 Å, Human ESCRT-I heterotetramer headpiece
4EJE 2.2 Å, Structure Of The Tsg101 UEV Domain In Complex With an Ebola PTAP late Domain Peptide
7ZLX 2.25 Å, Crystal Structure of the TSG101-UEV domain:space group P21
2F0R 2.26 Å, Crystallographic structure of human Tsg101 UEV domain

Browse structure collections

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