Research workbench
Monoclinic form of human C-reactive protein
Analyse Monoclinic form of human C-reactive protein in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3PVO
- Type
- protein
- Length
- 4,120 residues
- Chains
- 20
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- C-reactive protein
- UniProt
- P02741
- Ligands
- CA
- Pockets
- 20 · best druggability 0.67
Structure
x-ray diffraction · 1 distinct chain · 9% helix, 45% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D, E, F, G, H, I, J, K, L, M, N, O, P, Q, R, S, T | C-reactive protein | protein | 206 | 9% helix, 45% strand | P02741 |
Ligands and binding sites
- CA · Calcium ion · metal · 40 copies · chains A, B, C, D, E, F, G, H, I, J, K, L, M, N, O, P, Q, R, S, T
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
20 pockets found on a 1 Å grid, 15 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 667 | 0.67 | 0.76 | 66 | empty |
| 2 | 357 | 0.58 | 0.76 | 62 | empty |
| 3 | 291 | 0.56 | 0.76 | 46 | empty |
| 4 | 296 | 0.55 | 0.76 | 59 | empty |
| 5 | 285 | 0.55 | 0.76 | 54 | empty |
Interfaces
22 interfaces between chains.
- G–H · 724 Ų buried · 12 hydrogen bonds · protein-protein
- N–O · 720 Ų buried · 11 hydrogen bonds · protein-protein
- D–E · 717 Ų buried · 11 hydrogen bonds · protein-protein
- I–J · 716 Ų buried · 10 hydrogen bonds · protein-protein
- K–L · 712 Ų buried · 12 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 20 disulfide (disulfide).
Compared structures
- 3PVO · Monoclinic form of Human C-Reactive Protein · the same entry in another collection · chain J against J, 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 P02741
- Elsewhere: RCSB PDB 3PVO · PDBe 3PVO · UniProt P02741
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