Research workbench
Crystal structure of chaetomium thermophilum NIC96 sol-NUP53 complex
Analyse Crystal structure of chaetomium thermophilum NIC96 sol-NUP53 complex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5HB3
- Type
- protein
- Length
- 1,447 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- G0S024, G0S156
Structure
x-ray diffraction · 4 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 703 | — | G0S024 |
| B | — | protein | 18 | — | G0S156 |
| C | — | protein | 709 | — | G0S024 |
| D | — | protein | 17 | — | G0S156 |
Compared structures
- 5HB3 · Crystal structure of Chaetomium thermophilum Nic96 SOL-Nup53 complex · the same entry in another collection · chain D against D, TM-score 1.00
- G0S024 · AlphaFold monomer V2.0 prediction for nucleoporin NIC96 (G0S024) · a predicted model of the same protein · chain A against A, TM-score 0.98
- G0S156 · AlphaFold monomer V2.0 prediction for nucleoporin NUP53 (G0S156) · a predicted model of the same protein · chain B against A, TM-score 0.77
Analyse
- Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
- Every structure of UniProt G0S024
- Every structure of UniProt G0S156
- Elsewhere: RCSB PDB 5HB3 · PDBe 5HB3 · UniProt G0S024 · UniProt G0S156
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