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The crystal structure of full length IPAH9.8

Analyse The crystal structure of full length IPAH9.8 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6LOL
Type: protein
Length: 466 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: E3 ubiquitin-protein ligase IPAH9.8
EC: 2.3.2.27
UniProt: D2AJU0
Pockets: 2 · best druggability 0.74

Structure

x-ray diffraction · 1 distinct chain · 41% helix, 7% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	E3 ubiquitin-protein ligase IPAH9.8 (EC 2.3.2.27)	protein	466	41% helix, 7% strand	D2AJU0

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	789	0.74	0.79	69	empty
2	55	0.29	0.75	14	empty

Compared structures

6LOL · The crystal structure of full length IpaH9.8 · the same entry in another collection · chain A against A, TM-score 1.00
D2AJU0 · AlphaFold monomer V2.0 prediction for E3 ubiquitin-protein ligase IPAH9.8 (D2AJU0) · a predicted model of the same protein · chain A against A, TM-score 0.88

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 D2AJU0
Elsewhere: RCSB PDB 6LOL · PDBe 6LOL · UniProt D2AJU0

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