Research workbench

Human C-reactive protein

Analyse 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: 1GNH
Type: protein
Length: 2,060 residues
Chains: 10
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: C-reactive protein
UniProt: P02741
Ligands: CA
Pockets: 20 · best druggability 0.59

Structure

x-ray diffraction · 1 distinct chain · 9% helix, 44% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B, C, D, E, F, G, H, I, J	C-reactive protein	protein	206	9% helix, 44% strand	P02741

Ligands and binding sites

CA · Calcium ion · metal · 16 copies · chains A, B, C, E, F, G, H, I

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

Pockets

20 pockets found on a 1 Å grid, 6 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	330	0.59	0.77	52	empty
2	230	0.55	0.78	41	empty
3	258	0.52	0.75	44	empty
4	170	0.51	0.78	33	empty
5	218	0.51	0.76	33	empty

Interfaces

10 interfaces between chains.

A–B · 743 Å² buried · 11 hydrogen bonds · protein-protein
F–G · 725 Å² buried · 11 hydrogen bonds · protein-protein
I–J · 706 Å² buried · 8 hydrogen bonds · protein-protein
C–D · 706 Å² buried · 8 hydrogen bonds · protein-protein
H–I · 698 Å² buried · 9 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 10 disulfide (disulfide).

Compared structures

1GNH · Human C-reactive protein · the same entry in another collection · chain J against J, TM-score 1.00
P02741 · AlphaFold monomer V2.0 prediction for C-reactive protein (P02741) · a predicted model of the same protein · chain G 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 1GNH · PDBe 1GNH · UniProt P02741

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