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Cryoem reconstruction of human IKK1, open conformation 1

Analyse Cryoem reconstruction of human IKK1, open conformation 1 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5TQW
Type: protein
Length: 1,128 residues
Chains: 2
Method: electron microscopy
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Inhibitor of nuclear factor kappa-B kinase subunit alpha
EC: 2.7.11.10
UniProt: O15111
Pockets: 13 · best druggability 0.75

Structure

electron microscopy · 1 distinct chain · 60% helix, 9% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Inhibitor of nuclear factor kappa-B kinase subunit alpha (EC 2.7.11.10)	protein	564	60% helix, 9% strand	O15111

Pockets

13 pockets found on a 1 Å grid, 7 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	1174	0.75	0.78	116	empty
2	243	0.74	0.88	46	empty
3	447	0.71	0.81	47	empty
4	98	0.62	0.88	24	empty
5	346	0.60	0.77	43	empty

Interfaces

1 interface between chains.

A–B · 1162 Å² buried · 4 hydrogen bonds · protein-protein

Compared structures

5TQW · CryoEM reconstruction of human IKK1, open conformation 1 · the same entry in another collection · chain A against A, TM-score 1.00
O15111 · AlphaFold monomer V2.0 prediction for inhibitor of nuclear factor kappa-B kinase subunit… · a predicted model of the same protein · chain A against A, TM-score 0.96

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 O15111
Elsewhere: RCSB PDB 5TQW · PDBe 5TQW · UniProt O15111

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