Research workbench
Escherichia COLI dps
Analyse Escherichia COLI dps in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6QVX
- Type
- protein
- Length
- 3,729 residues
- Chains
- 24
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P0ABT2
- Ligands
- SO4
Structure
x-ray diffraction · 4 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D, F, G, H, I, L, N, P, Q, U, V, X | — | protein | 155 | — | P0ABT2 |
| E, J, M, O, R, T, W | — | protein | 156 | — | P0ABT2 |
| K | — | protein | 154 | — | P0ABT2 |
| S | — | protein | 158 | — | P0ABT2 |
Ligands and binding sites
- SO4 · Sulfate ion · ion · 50 copies · chains A, I, E, B, H, K, C, L, D, G, F, J, M, Q, U, N, T, W, O, P, S, X, R, V
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- P0ABT2 · AlphaFold monomer V2.0 prediction for DNA protection during starvation protein (P0ABT2) · a predicted model of the same protein · chain F 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 P0ABT2
- Elsewhere: RCSB PDB 6QVX · PDBe 6QVX · UniProt P0ABT2
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