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Structure of the N-terminal domain and the D1 aaa domain of membrane fusion ATPase P97

Analyse Structure of the N-terminal domain and the D1 aaa domain of membrane fusion… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1E32
Type: protein
Length: 438 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: P97
UniProt: Q01853
Ligands: ADP
Pockets: 5 · best druggability 0.57

Structure

x-ray diffraction · 1 distinct chain · 36% helix, 22% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	P97	protein	438	36% helix, 22% strand	Q01853

Ligands and binding sites

ADP · Adenosine-5'-diphosphate · ligand · chains A

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

5 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	354	0.57	0.76	40	empty
2	78	0.45	0.82	25	empty
3	197	0.44	0.73	33	empty
4	96	0.44	0.79	25	ADP
5	58	0.38	0.80	18	empty

Compared structures

1E32 · Structure of the N-Terminal domain and the D1 AAA domain of membrane fusion ATPase p97 · the same entry in another collection · chain A against A, TM-score 1.00
Q01853 · AlphaFold monomer V2.0 prediction for transitional endoplasmic reticulum ATPase (Q01853) · a predicted model of the same protein · chain A against A, TM-score 0.97

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Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
Every structure of UniProt Q01853
Elsewhere: RCSB PDB 1E32 · PDBe 1E32 · UniProt Q01853

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