MolNFT v1 · #136560 · protein
Crystal structure of SMAD4 nes peptide in complex with CRM1-ran-RANBP1
5UWU: “Crystal structure of SMAD4 nes peptide in complex with CRM1-ran-RANBP1”. X-ray diffraction, 3 ligands (GNP, MG, CL). MolNFT v1 #136560 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 5UWU
- Type
- protein
- Length
- 1,345 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P62826, P41920, P30822
- Ligands
- GNP, MG, CL
Structure
x-ray diffraction · 4 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 208 | — | P62826 |
| B | — | protein | 130 | — | P41920 |
| C | — | protein | 998 | — | P30822 |
| D | — | protein | 9 | — | — |
Ligands and binding sites
- GNP · Phosphoaminophosphonic acid-guanylate ester · ligand · chains A
- MG · Magnesium ion · metal · chains A
- CL · Chloride ion · ion · chains C
- GOL · Glycerol · additive · 3 copies · chains A, C
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 5UWU · Crystal Structure of SMAD4 NES Peptide in complex with CRM1-Ran-RanBP1 · the same entry in another collection · chain A against A, TM-score 1.00
- P30822 · AlphaFold monomer V2.0 prediction for exportin-1 (P30822) · a predicted model of the same protein · chain C against A, TM-score 0.98
- P41920 · AlphaFold monomer V2.0 prediction for ran-specific GTPase-activating protein 1 (P41920) · a predicted model of the same protein · chain B against A, TM-score 0.94
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 P62826
- Every structure of UniProt P41920
- Every structure of UniProt P30822
- Elsewhere: RCSB PDB 5UWU · PDBe 5UWU · UniProt P62826 · UniProt P41920 · UniProt P30822
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