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The crystal structure of murine P97/VCP at 3.6A

Analyse The crystal structure of murine P97/VCP at 3.6A in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1R7R
Type: protein
Length: 683 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Transitional endoplasmic reticulum ATPase
UniProt: Q01853
Ligands: ADP
Pockets: 9 · best druggability 0.73

Structure

x-ray diffraction · 1 distinct chain · 39% helix, 18% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Transitional endoplasmic reticulum ATPase	protein	683	39% helix, 18% 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

9 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	595	0.73	0.81	65	empty
2	542	0.66	0.77	81	empty
3	307	0.60	0.78	42	empty
4	280	0.58	0.78	46	empty
5	70	0.44	0.82	24	empty

Compared structures

1R7R · The crystal structure of murine p97/VCP at 3.6A · 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 0.80

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 Q01853
Elsewhere: RCSB PDB 1R7R · PDBe 1R7R · UniProt Q01853

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