Research workbench
Structure of truncated ccpa in complex with P-ser-hpr and sulfate ions
Analyse Structure of truncated ccpa in complex with P-ser-hpr and sulfate ions in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2FEP
- Type
- protein
- Length
- 360 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P25144, P08877
Structure
x-ray diffraction · 2 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 273 | — | P25144 |
| S | — | protein | 87 | — | P08877 |
Compared structures
- 2FEP · Structure of truncated CcpA in complex with P-Ser-HPr and Sulfate ions · the same entry in another collection · chain A against A, TM-score 1.00
- P25144 · AlphaFold monomer V2.0 prediction for catabolite control protein a (P25144) · a predicted model of the same protein · chain A against A, TM-score 0.99
- P08877 · AlphaFold monomer V2.0 prediction for phosphocarrier protein hpr (P08877) · a predicted model of the same protein · chain S against A, TM-score 0.99
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 P25144
- Every structure of UniProt P08877
- Elsewhere: RCSB PDB 2FEP · PDBe 2FEP · UniProt P25144 · UniProt P08877
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