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C-reactive protein decamer at pH 7.5

Analyse C-reactive protein decamer at pH 7.5 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 7PK9
Type: protein
Length: 2,060 residues
Chains: 10
Method: electron microscopy
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: C-reactive protein
UniProt: P02741
Ligands: CA
Pockets: 20 · best druggability 0.78

Structure

electron microscopy · 1 distinct chain · 9% helix, 45% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
J, F, G, H, I, E, D, C, B, A	C-reactive protein	protein	206	9% helix, 45% strand	P02741

Ligands and binding sites

CA · Calcium ion · metal · 20 copies · chains J, F, G, H, I, E, D, C, B, A

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

20 pockets found on a 1 Å grid, 7 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	1152	0.78	0.80	103	empty
2	787	0.78	0.81	109	empty
3	724	0.77	0.81	92	empty
4	149	0.57	0.82	23	empty
5	309	0.55	0.75	46	empty

Interfaces

16 interfaces between chains.

G–H · 770 Å² buried · 9 hydrogen bonds · protein-protein
H–I · 714 Å² buried · 7 hydrogen bonds · protein-protein
C–B · 712 Å² buried · 11 hydrogen bonds · protein-protein
D–C · 699 Å² buried · 11 hydrogen bonds · protein-protein
F–G · 696 Å² buried · 10 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 10 disulfide (disulfide).

Compared structures

7PK9 · C-reactive protein decamer at pH 7.5 · the same entry in another collection · chain A against A, TM-score 1.00
P02741 · AlphaFold monomer V2.0 prediction for C-reactive protein (P02741) · 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 P02741
Elsewhere: RCSB PDB 7PK9 · PDBe 7PK9 · UniProt P02741

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