Research workbench
Sfgfp 204-204 mutant dimer
Analyse Sfgfp 204-204 mutant dimer in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5NI3
- Type
- protein
- Length
- 904 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- A0A059PIQ0
- Ligands
- CRO, DB5, NA, CL
Structure
x-ray diffraction · 4 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 224 | — | A0A059PIQ0 |
| B | — | protein | 228 | — | A0A059PIQ0 |
| C | — | protein | 228 | — | A0A059PIQ0 |
| D | — | protein | 224 | — | A0A059PIQ0 |
Ligands and binding sites
- CRO · {2-[(1R,2R)-1-amino-2-hydroxypropyl]-4-(4-hydroxybenzylidene)-5-oxo-4,5-dihydro-1H-imidazol-1-yl}acetic acid · ligand · 4 copies · chains A, B, C, D
- DB5 · [(4~{S})-4,5,6,7,8,9-hexahydro-1~{H}-cycloocta[d][1,2, 3]triazol-4-yl] hydrogen carbonate · ligand · 2 copies · chains A, D, B, C
- NA · Sodium ion · metal · 10 copies · chains A, B, C, D
- CL · Chloride ion · ion · chains C
- GOL · Glycerol · additive · 5 copies · chains B, C, D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 5NI3 · sfGFP 204-204 mutant dimer · 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 A0A059PIQ0
- Elsewhere: RCSB PDB 5NI3 · PDBe 5NI3 · UniProt A0A059PIQ0
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