Research workbench

Structure of RIP2 card domain

Analyse Structure of RIP2 card domain in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5YRN
Type: protein
Length: 1,044 residues
Chains: 12
Method: electron microscopy
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Receptor-interacting SERINE/THREONINE-protein kinase 2
EC: 2.7.11.1, 2.7.10.2
UniProt: O43353
Pockets: 17 · best druggability 0.79

Structure

electron microscopy · 1 distinct chain · 75% helix, 0% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B, C, D, E, F, G, H, I, J, K, L	Receptor-interacting SERINE/THREONINE-protein kinase 2 (EC 2.7.11.1, 2.7.10.2)	protein	87	75% helix, 0% strand	O43353

Pockets

17 pockets found on a 1 Å grid, 8 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	769	0.79	0.83	102	empty
2	608	0.77	0.84	81	empty
3	475	0.66	0.78	47	empty
4	482	0.65	0.78	55	empty
5	455	0.64	0.77	48	empty

Interfaces

28 interfaces between chains.

B–E · 446 Å² buried · 6 hydrogen bonds · protein-protein
C–I · 446 Å² buried · 5 hydrogen bonds · protein-protein
A–J · 430 Å² buried · 2 hydrogen bonds · protein-protein
G–H · 430 Å² buried · 2 hydrogen bonds · protein-protein
B–C · 427 Å² buried · 3 hydrogen bonds · protein-protein

Compared structures

5YRN · Structure of RIP2 CARD domain · the same entry in another collection · chain L against L, 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 O43353
Elsewhere: RCSB PDB 5YRN · PDBe 5YRN · UniProt O43353

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