MolNFT v1 · #71013 · protein
Crystal structure of yeast CRM1 (XPO1P) in complex with yeast RANBP1 (YRB1P) and yeast rangtp (GSP1PGTP)
3M1I: “Crystal structure of yeast CRM1 (XPO1P) in complex with yeast RANBP1 (YRB1P) and yeast rangtp (GSP1PGTP)”. X-ray diffraction. MolNFT v1 #71013 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 3M1I
- Type
- protein
- Length
- 1,354 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P32835, P41920, P30822
Structure
x-ray diffraction · 3 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 200 | — | P32835 |
| B | — | protein | 131 | — | P41920 |
| C | — | protein | 1023 | — | P30822 |
Compared structures
- 3M1I · Crystal structure of yeast CRM1 (Xpo1p) in complex with yeast RanBP1 (Yrb1p) and yeast… · the same entry in another collection · chain A against A, TM-score 1.00
- 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 0.99
- 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
- P32835 · AlphaFold monomer V2.0 prediction for GTP-binding nuclear protein GSP1/CNR1 (P32835) · a predicted model of the same protein · chain A against A, TM-score 0.85
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 P32835
- Every structure of UniProt P41920
- Every structure of UniProt P30822
- Elsewhere: RCSB PDB 3M1I · PDBe 3M1I · UniProt P32835 · UniProt P41920 · UniProt P30822
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.