MolNFT v1 · #136554 · protein
Crystal structure of engineered fmrp-1B nes peptide in complex with CRM1-ran-RANBP1
5UWO: “Crystal structure of engineered fmrp-1B nes peptide in complex with CRM1-ran-RANBP1”. X-ray diffraction, 2 ligands (GNP, MG). MolNFT v1 #136554 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 5UWO
- Type
- protein
- Length
- 1,339 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P62826, P41920, P30822
- Ligands
- GNP, MG
Structure
x-ray diffraction · 4 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 205 | — | P62826 |
| B | — | protein | 128 | — | P41920 |
| C | — | protein | 996 | — | P30822 |
| D | — | protein | 10 | — | — |
Ligands and binding sites
- GNP · Phosphoaminophosphonic acid-guanylate ester · ligand · chains A
- MG · Magnesium ion · metal · chains A
- GOL · Glycerol · additive · 2 copies · chains A, C
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 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 5UWO · PDBe 5UWO · UniProt P62826 · UniProt P41920 · UniProt P30822
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