Research workbench

Crystal structure of the P97 D2 domain in a helical split-washer conformation

Analyse Crystal structure of the P97 D2 domain in a helical split-washer conformation in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6G2V
Type: protein
Length: 266 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Transitional endoplasmic reticulum ATPase
EC: 3.6.4.6
UniProt: P55072
Ligands: ADP
Pockets: 4 · best druggability 0.69

Structure

x-ray diffraction · 1 distinct chain · 55% helix, 12% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Transitional endoplasmic reticulum ATPase (EC 3.6.4.6)	protein	266	55% helix, 12% strand	P55072

Ligands and binding sites

ADP · Adenosine-5'-diphosphate · ligand · chains A
MPD · (4S)-2-methyl-2,4-pentanediol · additive · 4 copies · chains A
DMS · Dimethyl sulfoxide · additive · chains A

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

Pockets

4 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	90	0.69	0.92	20	MPD
2	174	0.53	0.78	23	MPD
3	64	0.41	0.80	11	MPD
4	90	0.39	0.77	24	ADP

Compared structures

6G2V · Crystal structure of the p97 D2 domain in a helical split-washer conformation · the same entry in another collection · chain A against A, TM-score 1.00

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 P55072
Elsewhere: RCSB PDB 6G2V · PDBe 6G2V · UniProt P55072

GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.