Research workbench
On the routine use of soft X-rays in macromolecular crystallography, part III- the optimal data collection wavelength
Analyse On the routine use of soft X-rays in macromolecular crystallography, part III… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2A7B
- Type
- protein
- Length
- 120 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Gamma-adaptin appendage domain
- UniProt
- P22892
- Ligands
- XE
Structure
x-ray diffraction · 1 distinct chain · 5% helix, 54% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Gamma-adaptin appendage domain | protein | 120 | 5% helix, 54% strand | P22892 |
Ligands and binding sites
- XE · Xenon · ion · 2 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 2A7B · On the Routine Use of Soft X-Rays in Macromolecular Crystallography, Part III- The… · the same entry in another collection · chain A against A, TM-score 1.00
- P22892 · AlphaFold monomer V2.0 prediction for ap-1 complex subunit gamma-1 (P22892) · a predicted model of the same protein · chain A against A, TM-score 0.98
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 P22892
- Elsewhere: RCSB PDB 2A7B · PDBe 2A7B · UniProt P22892
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