Research workbench
Selenomethionine mutant (V29SEM) of protein GB1 examined by X-ray diffraction
Analyse Selenomethionine mutant (V29SEM) of protein GB1 examined by X-ray diffraction in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6C9O
- Type
- protein
- Length
- 112 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Immunoglobulin G-binding protein G
- UniProt
- P19909
Structure
x-ray diffraction · 1 distinct chain · 25% helix, 43% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Immunoglobulin G-binding protein G | protein | 56 | 25% helix, 43% strand | P19909 |
Ligands and binding sites
- MPD · (4S)-2-methyl-2,4-pentanediol · additive · 4 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Interfaces
1 interface between chains.
- A–B · 70 Ų buried · 1 hydrogen bond · protein-protein
Modifications
Observed in the structure: 2 modified (engineered).
Compared structures
- 6C9O · Selenomethionine mutant (V29Sem) of protein GB1 examined by 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 0.97
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 6C9O · PDBe 6C9O · UniProt P19909
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