MolNFT v1 · #2657 · protein

X-ray crystal structure of C3D: a C3 fragment and ligand for complement receptor 2

1C3D: “X-ray crystal structure of C3D: a C3 fragment and ligand for complement receptor 2”. X-ray diffraction, 3 pockets (best druggability 0.49). MolNFT v1 #2657 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 1C3D
Type: protein
Length: 294 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: C3D
UniProt: P01024
Pockets: 3 · best druggability 0.49

Structure

x-ray diffraction · 1 distinct chain · 63% helix, 2% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	C3D	protein	294	63% helix, 2% strand	P01024

Ligands and binding sites

GOL · Glycerol · additive · 5 copies · chains A

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

Pockets

3 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	102	0.49	0.81	17	GOL
2	161	0.43	0.74	24	empty
3	52	0.28	0.74	17	GOL

Modifications

Observed in the structure: 1 disulfide (disulfide).

Compared structures

1C3D · X-ray crystal structure of C3D: a C3 fragment and ligand for complement receptor 2 · the same entry in another collection · chain A against A, TM-score 1.00
P01024 · AlphaFold monomer V2.0 prediction for complement C3 (P01024) · a predicted model of the same protein · chain A against A, TM-score 0.90

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 P01024
Elsewhere: RCSB PDB 1C3D · PDBe 1C3D · UniProt P01024

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