Research workbench

Crystal structure of human complement protein C8GAMMA with laurate

Analyse Crystal structure of human complement protein C8GAMMA with laurate in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2OVD
Type: protein
Length: 162 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Complement component 8, gamma polypeptide
UniProt: Q14CU0
Ligands: DAO
Pockets: 1 · best druggability 0.69

Structure

x-ray diffraction · 1 distinct chain · 17% helix, 45% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Complement component 8, gamma polypeptide	protein	162	17% helix, 45% strand	Q14CU0

Ligands and binding sites

DAO · Lauric acid · ligand · chains A

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

Pockets

1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	359	0.69	0.81	40	DAO

Modifications

Observed in the structure: 1 disulfide (disulfide).

Compared structures

2OVD · Crystal Structure of Human Complement Protein C8gamma with Laurate · the same entry in another collection · chain A 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 Q14CU0
Elsewhere: RCSB PDB 2OVD · PDBe 2OVD · UniProt Q14CU0

GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.