Research workbench

The poly-C9 component of the complement membrane attack complex

Analyse The poly-C9 component of the complement membrane attack complex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5FMW
Type: protein
Length: 10,582 residues
Chains: 22
Method: electron microscopy
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: POLYC9
UniProt: P02748
Pockets: 5 · best druggability 0.33

Structure

electron microscopy · 1 distinct chain · 0% helix, 0% 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, U, V	POLYC9	protein	481	0% helix, 0% strand	P02748

Pockets

5 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	82	0.33	0.72	25	empty
2	73	0.30	0.71	29	empty
3	52	0.30	0.74	14	empty
4	60	0.30	0.73	21	empty
5	52	0.27	0.72	19	empty

Interfaces

22 interfaces between chains.

J–K · 601 Å² buried · 0 hydrogen bonds · protein-protein
L–M · 601 Å² buried · 0 hydrogen bonds · protein-protein
S–T · 601 Å² buried · 0 hydrogen bonds · protein-protein
Q–R · 601 Å² buried · 0 hydrogen bonds · protein-protein
C–D · 601 Å² buried · 0 hydrogen bonds · protein-protein

Compared structures

5FMW · The poly-C9 component of the Complement Membrane Attack Complex · the same entry in another collection · chain K against K, 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 P02748
Elsewhere: RCSB PDB 5FMW · PDBe 5FMW · UniProt P02748

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