Research workbench
The solution structure of human DOCK2 SH3 domain - ELMO1 peptide chimera complex
Analyse The solution structure of human DOCK2 SH3 domain - ELMO1 peptide chimera complex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2RQR
- Type
- protein
- Length
- 119 residues
- Chains
- 1
- Method
- solution nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Engulfment and cell motility protein 1,DEDICATOR of cytokinesis protein 2
- UniProt
- Q92556, Q92608
Structure
solution nmr · 1 distinct chain · 3% helix, 24% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Engulfment and cell motility protein 1,DEDICATOR of cytokinesis protein 2 | protein | 119 | 3% helix, 24% strand | Q92556, Q92608 |
Compared structures
- 2RQR · The solution structure of human DOCK2 SH3 domain - ELMO1 peptide chimera complex · the same entry in another collection · chain A against A, TM-score 1.00
- Q92608 · AlphaFold monomer V2.0 prediction for dedicator of cytokinesis protein 2 (Q92608) · a predicted model of the same protein · chain A against A, TM-score 0.49
- Q92556 · AlphaFold monomer V2.0 prediction for engulfment and cell motility protein 1 (Q92556) · a predicted model of the same protein · chain A against A, TM-score 0.38
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 Q92556
- Every structure of UniProt Q92608
- Elsewhere: RCSB PDB 2RQR · PDBe 2RQR · UniProt Q92556 · UniProt Q92608
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