MolNFT v1 · #439612 · protein
AlphaFold monomer V2.0 prediction for stromal interaction molecule 1 (Q13586)
Q13586: “AlphaFold monomer V2.0 prediction for stromal interaction molecule 1 (Q13586)”. 1 pocket (best druggability 0.29). MolNFT v1 #439612 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- Accession
- Q13586
- Type
- protein
- Length
- 685 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x922634802C3497a6A458944C1356490ce4100c17
- Molecule
- Stromal interaction molecule 1
- UniProt
- Q13586
- Pockets
- 1 · best druggability 0.29
Structure
1 distinct chain · 50% helix, 1% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Stromal interaction molecule 1 | protein | 685 | 50% helix, 1% strand | Q13586 |
Pockets
1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 60 | 0.29 | 0.73 | 8 | empty |
Modifications
Observed in the structure: 1 disulfide (disulfide).
Compared structures
- 2K60 · NMR structure of calcium-loaded STIM1 EF-SAM · an experimental structure of the same protein · chain A against A, TM-score 0.20
- 2K60 · NMR structure of calcium-loaded STIM1 ef-SAM · an experimental structure of the same protein · chain A against A, TM-score 0.20
- 3TEQ · Crystal structure of soar domain · an experimental structure of the same protein · chain A against B, TM-score 0.13
- 3TEQ · Crystal structure of SOAR domain · an experimental structure of the same protein · chain A against B, TM-score 0.13
- 4O9B · The structure of CC1-ih in human STIM1. · an experimental structure of the same protein · chain A against C, TM-score 0.12
- 4O9B · The Structure of CC1-IH in human STIM1. · an experimental structure of the same protein · chain A against C, TM-score 0.12
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 Q13586
- Elsewhere: UniProt Q13586 · AlphaFold DB Q13586
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