2GWF: USP8-NRDP1 complex
Structure of a USP8-NRDP1 complex. Determined by X-ray diffraction at 2.3 Å resolution. Released 6 Jun 2006.
- Method
- X-ray diffraction
- Resolution
- 2.3 Å
- Organism
- Homo sapiens
- Chains
- 6
- Atoms
- 6,388
- Mol. weight
- 98.29 kDa
- Released
- 6 Jun 2006
Explore 2GWF in 3D
Show helices and sheets
RCSB PDB
PDBe
Secondary structure: helices and β-sheets
2GWF contains 57 α-helices and 43 β-strands across 6 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: 9 helices, 7 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 182-183 | 2 | 1 |
| α-helix | 185-193 | 9 | |
| β-strand | 199-203 | 5 | 1 |
| α-helix | 207-212 | 6 | |
| β-strand | 215 | 1 | 2 |
| β-strand | 219-220 | 2 | 1 |
| α-helix | 223-225 | 3 | |
| α-helix | 232-237 | 6 | |
| α-helix | 241-248 | 8 | |
| β-strand | 255-259 | 5 | 1 |
| α-helix | 265-267 | 3 | |
| α-helix | 273-282 | 10 | |
| β-strand | 295-297 | 3 | 1 |
| α-helix | 300-307 | 8 | |
| α-helix | 309-311 | 3 | |
| β-strand | 312 | 1 | 2 |
Chain B: 10 helices, 7 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 198-205 | 8 | |
| α-helix | 207 | 1 | |
| β-strand | 208 | 1 | 3 |
| β-strand | 209-211 | 3 | 4 |
| α-helix | 214-216 | 3 | |
| β-strand | 217-218 | 2 | 3 |
| α-helix | 223-235 | 13 | |
| α-helix | 240-248 | 9 | |
| α-helix | 252-254 | 3 | |
| α-helix | 257-259 | 3 | |
| α-helix | 262-272 | 11 | |
| β-strand | 278-279 | 2 | 3 |
| α-helix | 280 | 1 | |
| β-strand | 285-289 | 5 | 3 |
| α-helix | 290-292 | 3 | |
| β-strand | 305-310 | 6 | 3 |
| β-strand | 314-316 | 3 | 4 |
Chain C: 10 helices, 7 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 182-183 | 2 | 5 |
| α-helix | 185-193 | 9 | |
| β-strand | 199-203 | 5 | 5 |
| α-helix | 207-212 | 6 | |
| β-strand | 215 | 1 | 6 |
| α-helix | 218 | 1 | |
| β-strand | 219-220 | 2 | 5 |
| α-helix | 223-225 | 3 | |
| α-helix | 232-237 | 6 | |
| α-helix | 241-247 | 7 | |
| β-strand | 255-259 | 5 | 5 |
| α-helix | 265-267 | 3 | |
| α-helix | 273-282 | 10 | |
| β-strand | 295-297 | 3 | 5 |
| α-helix | 300-307 | 8 | |
| α-helix | 309-311 | 3 | |
| β-strand | 312 | 1 | 6 |
Chain D: 9 helices, 7 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 193-205 | 13 | |
| α-helix | 207 | 1 | |
| β-strand | 208 | 1 | 7 |
| β-strand | 209-211 | 3 | 8 |
| α-helix | 214-216 | 3 | |
| β-strand | 217-218 | 2 | 7 |
| α-helix | 223-235 | 13 | |
| α-helix | 243-248 | 6 | |
| α-helix | 252-254 | 3 | |
| α-helix | 262-268 | 7 | |
| α-helix | 269-274 | 6 | |
| β-strand | 278-279 | 2 | 7 |
| β-strand | 285-289 | 5 | 7 |
| α-helix | 290-292 | 3 | |
| β-strand | 305-310 | 6 | 7 |
| β-strand | 314-316 | 3 | 8 |
Chain E: 10 helices, 8 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 182-183 | 2 | 9 |
| α-helix | 185-193 | 9 | |
| β-strand | 199-203 | 5 | 9 |
| α-helix | 207-212 | 6 | |
| β-strand | 215 | 1 | 10 |
| α-helix | 218 | 1 | |
| β-strand | 219-220 | 2 | 9 |
| α-helix | 223-225 | 3 | |
| α-helix | 232-237 | 6 | |
| α-helix | 241-248 | 8 | |
| β-strand | 255-259 | 5 | 9 |
| α-helix | 265-267 | 3 | |
| α-helix | 273-282 | 10 | |
| β-strand | 295-297 | 3 | 9 |
| α-helix | 300-307 | 8 | |
| α-helix | 309-311 | 3 | |
| β-strand | 312 | 1 | 10 |
| β-strand | 314 | 1 | 10 |
Chain F: 9 helices, 7 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 197-205 | 9 | |
| α-helix | 207 | 1 | |
| β-strand | 208 | 1 | 11 |
| β-strand | 209-211 | 3 | 12 |
| α-helix | 214-216 | 3 | |
| β-strand | 217-218 | 2 | 11 |
| α-helix | 223-235 | 13 | |
| α-helix | 240-248 | 9 | |
| α-helix | 252-254 | 3 | |
| α-helix | 262-268 | 7 | |
| α-helix | 269-274 | 6 | |
| β-strand | 277-279 | 3 | 11 |
| β-strand | 285-289 | 5 | 11 |
| α-helix | 290-292 | 3 | |
| β-strand | 305-310 | 6 | 11 |
| β-strand | 314-316 | 3 | 12 |
Molecules and chains
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|
| Ubiquitin carboxyl-terminal hydrolase 8 | A, C, E | protein | 157 | Homo sapiens | P40818 (AlphaFold model) |
| RING finger protein 41 | B, D, F | protein | 134 | Homo sapiens | Q9H4P4 (AlphaFold model) |
Sequence of entity 1 (A, C, E), FASTA
>2GWF_1 Ubiquitin carboxyl-terminal hydrolase 8 (chains A, C, E)
MGSSHHHHHHSSGLVPRGSGAITAKELYTMMTDKNISLIIMDARRMQDYQDSCILHSLSV
PEEAISPGVTASWIEAHLPDDSKDTWKKRGNVEYVVLLDWFSSAKDLQIGTTLRSLKDAL
FKWESKTVLRNEPLVLEGGYENWLLCYPQYTTNAKVT
Sequence of entity 2 (B, D, F), FASTA
>2GWF_2 RING finger protein 41 (chains B, D, F)
SSGLVPRGSTIEYNEILEWVNSLQPARVTRWGGMISTPDAVLQAVIKRSLVESGCPASIV
NELIENAHERSWPQGLATLETRQMNRRYYENYVAKRIPGKQAVVVMACENQHMGDDMVQE
PGLVMIFAHGVEEI
Primary citation
Amino-terminal Dimerization, NRDP1-Rhodanese Interaction, and Inhibited Catalytic Domain Conformation of the Ubiquitin-specific Protease 8 (USP8). Avvakumov, G.V., Walker, J.R., Xue, S. et al. J Biol Chem (2006) 281:38061-38070. DOI 10.1074/jbc.M606704200 · PubMed
Other PDB entries of the same protein (UniProt P40818 (AlphaFold model), which also has an AlphaFold model), best resolution first:
- 6F09 1.59 Å, Binary complex of 14-3-3 zeta with ubiquitin specific protease 8 (USP8) pSer718 peptide
- 8ADM 1.7 Å, Ternary complex of 14-3-3 sigma, Usp8pS718 phosphopeptide and small molecule stabilizer
- 2GFO 2.0 Å, Structure of the Catalytic Domain of Human Ubiquitin Carboxyl-terminal Hydrolase 8
- 2A9U 2.1 Å, Structure of the N-terminal domain of Human Ubiquitin carboxyl-terminal hydrolase 8 (USP8)
- 8XPN 2.1 Å, The Crystal Structure of USP8 from Biortus.
- 3N3K 2.6 Å, The catalytic domain of USP8 in complex with a USP8 specific inhibitor
- 8Y9A 3.1 Å, The Crystal Structure of USP8 from Biortus.
- 1WHB Solution structure of the Rhodanese-like domain in human ubiquitin specific protease 8…
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