Research workbench
Crystal structure of mutant achbp in complex with hepes (T53F, Q74R, Y110A, I135S, G162E)
Analyse Crystal structure of mutant achbp in complex with hepes (T53F, Q74R, Y110A… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5OAD
- Type
- protein
- Length
- 1,029 residues
- Chains
- 5
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- Q8WSF8
- Ligands
- NAG
Structure
x-ray diffraction · 3 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, C | — | protein | 206 | — | Q8WSF8 |
| B, D | — | protein | 205 | — | Q8WSF8 |
| E | — | protein | 207 | — | Q8WSF8 |
Ligands and binding sites
- NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 4 copies · chains A, B, C, D, E
- EPE · 4-(2-hydroxyethyl)-1-piperazine ethanesulfonic acid · additive · 3 copies · chains A, E, B, C, D
- EDO · 1,2-ethanediol · additive · 2 copies · chains B, C, D, E
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 5OAD · Crystal structure of mutant AChBP in complex with HEPES (T53F, Q74R, Y110A, I135S, G162E) · the same entry in another collection · chain A against A, TM-score 1.00
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 Q8WSF8
- Elsewhere: RCSB PDB 5OAD · PDBe 5OAD · UniProt Q8WSF8
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