Research workbench
Crystal polymorphism of protein GB1 examined by solid-state NMR and X- ray diffraction
Analyse Crystal polymorphism of protein GB1 examined by solid-state NMR and X- ray… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2QMT
- Type
- protein
- Length
- 56 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Immunoglobulin G-binding protein G
- UniProt
- P19909
- Ligands
- PO4
Structure
x-ray diffraction · 1 distinct chain · 25% helix, 43% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Immunoglobulin G-binding protein G | protein | 56 | 25% helix, 43% strand | P19909 |
Ligands and binding sites
- PO4 · Phosphate ion · ion · chains A
- IPA · Isopropyl alcohol · additive · 2 copies · chains A
- MRD · (4R)-2-methylpentane-2,4-diol · additive · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 2QMT · Crystal Polymorphism of Protein GB1 Examined by Solid-state NMR and X-ray Diffraction · the same entry in another collection · chain A against A, TM-score 1.00
- P19909 · AlphaFold monomer V2.0 prediction for immunoglobulin G-binding protein G (P19909) · a predicted model of the same protein · chain A against A, TM-score 0.96
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 P19909
- Elsewhere: RCSB PDB 2QMT · PDBe 2QMT · UniProt P19909
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