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Structure and activity of the N-terminal substrate recognition domains in proteasomal atpases - the arc domain structure

Analyse Structure and activity of the N-terminal substrate recognition domains in… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2WFW
Type: protein
Length: 373 residues
Chains: 3
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Arc
UniProt: O50202
Pockets: 2 · best druggability 0.71

Structure

x-ray diffraction · 2 distinct chains · 6% helix, 47% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, C	Arc	protein	124	7% helix, 48% strand	O50202
B	Arc	protein	125	6% helix, 47% strand	O50202

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	526	0.71	0.80	40	empty
2	567	0.71	0.79	48	empty

Interfaces

2 interfaces between chains.

A–C · 939 Å² buried · 16 hydrogen bonds · protein-protein
A–B · 882 Å² buried · 18 hydrogen bonds · protein-protein

Compared structures

2WFW · Structure and activity of the N-terminal substrate recognition domains in proteasomal… · the same entry in another collection · chain A against A, TM-score 1.00
O50202 · AlphaFold monomer V2.0 prediction for proteasome-associated ATPase (O50202) · a predicted model of the same protein · chain B against A, TM-score 0.97

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 O50202
Elsewhere: RCSB PDB 2WFW · PDBe 2WFW · UniProt O50202

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