Research workbench
Ccpa-hpr-SER46P-syn cre
Analyse Ccpa-hpr-SER46P-syn cre in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3OQO
- Type
- protein + DNA
- Length
- 871 residues
- Chains
- 6
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Catabolite control protein a; Phosphocarrier protein hpr…
- EC
- 2.7.11.-
- UniProt
- P25144, P08877
- Ligands
- SO4
- Pockets
- 12 · best druggability 0.75
Structure
x-ray diffraction · 5 distinct chains · 44% helix, 16% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Catabolite control protein a | protein | 333 | 46% helix, 15% strand | P25144 |
| S, D | Phosphocarrier protein hpr (EC 2.7.11.-) | protein | 87 | 36% helix, 23% strand | P08877 |
| C | Catabolite control protein a | protein | 332 | 45% helix, 15% strand | P25144 |
| E | 5'-D(*CP*TP*GP*TP*TP*AP*GP*CP*GP*CP*TP*TP*TP*CP*AP*G)-3' | dna | 16 | — | — |
| B | 5'-D(*CP*TP*GP*AP*AP*AP*GP*CP*GP*CP*TP*AP*AP*CP*AP*G)-3' | dna | 16 | — | — |
Ligands and binding sites
- SO4 · Sulfate ion · ion · 5 copies · chains A, S, C, D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
12 pockets found on a 1 Å grid, 6 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 684 | 0.75 | 0.81 | 74 | empty |
| 2 | 90 | 0.73 | 0.95 | 16 | empty |
| 3 | 607 | 0.72 | 0.80 | 64 | empty |
| 4 | 494 | 0.64 | 0.77 | 57 | SO4 |
| 5 | 230 | 0.57 | 0.79 | 26 | empty |
Interfaces
10 interfaces between chains.
- A–C · 2188 Ų buried · 34 hydrogen bonds · protein-protein
- E–B · 712 Ų buried · 70 hydrogen bonds · nucleic-nucleic
- C–D · 683 Ų buried · 6 hydrogen bonds · protein-protein
- A–S · 668 Ų buried · 8 hydrogen bonds · protein-protein
- A–B · 557 Ų buried · 9 hydrogen bonds · protein-nucleic
Modifications
Observed in the structure: 2 modified (phosphorylation).
Compared structures
- 3OQO · Ccpa-hpr-ser46p-syn cre · the same entry in another collection · chain B against B, 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 0.98
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 3OQO · PDBe 3OQO · UniProt P25144 · UniProt P08877
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