Research workbench
Structure of human C4b-binding protein alpha cain CCP domains 1 and 2 in complex with the hypervariable region of group A Streptococcus M28 protein
Analyse Structure of human C4b-binding protein alpha cain CCP domains 1 and 2 in… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5HYP
- Type
- protein
- Length
- 154 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 3.024
- Source
- Homo sapiens; Streptococcus pyogenes
- Molecule
- C4b-binding protein alpha chain; M28 protein
- UniProt
- P04003, W0T1Y4
- Pockets
- 1 · best druggability 0.30
Structure
x-ray diffraction · resolution 3.024 · 2 distinct chains · 16% helix, 34% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | C4b-binding protein alpha chain | protein | 125 | 0% helix, 42% strand | P04003 |
| B | M28 protein | protein | 29 | 86% helix, 0% strand | W0T1Y4 |
Pockets
1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 74 | 0.30 | 0.73 | 18 | empty |
Interfaces
1 interface between chains.
- A–B · 633 Ų buried · 12 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 4 disulfide (disulfide).
Compared structures
- 5HYP · Structure of human C4B-binding protein alpha cain ccp domains 1 and 2 in complex with the… · the same entry in another collection · chain A against A, TM-score 1.00
- P04003 · AlphaFold monomer V2.0 prediction for C4B-binding protein alpha chain (P04003) · a predicted model of the same protein · chain A against A, TM-score 0.93
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 P04003
- Every structure of UniProt W0T1Y4
- Elsewhere: RCSB PDB 5HYP · PDBe 5HYP · UniProt P04003 · UniProt W0T1Y4
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