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P97-R155H mutant dodecamer II

Analyse P97-R155H mutant dodecamer II in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 7L5X
Type: protein
Length: 6,384 residues
Chains: 12
Method: electron microscopy
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Transitional endoplasmic reticulum ATPase
EC: 3.6.4.6
UniProt: P55072
Pockets: 20 · best druggability 0.82

Structure

electron microscopy · 1 distinct chain · 52% helix, 10% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B, C, D, E, F, G, H, I, J, K, L	Transitional endoplasmic reticulum ATPase (EC 3.6.4.6)	protein	532	52% helix, 10% strand	P55072

Pockets

20 pockets found on a 1 Å grid, 20 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	1190	0.82	0.83	177	empty
2	919	0.81	0.83	147	empty
3	778	0.79	0.83	125	empty
4	1102	0.78	0.80	122	empty
5	704	0.78	0.83	103	empty

Interfaces

24 interfaces between chains.

J–K · 673 Å² buried · 1 hydrogen bond · protein-protein
B–C · 669 Å² buried · 1 hydrogen bond · protein-protein
C–D · 654 Å² buried · 1 hydrogen bond · protein-protein
I–J · 651 Å² buried · 1 hydrogen bond · protein-protein
K–L · 649 Å² buried · 1 hydrogen bond · protein-protein

Compared structures

7L5X · p97-R155H mutant dodecamer II · 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 7L5X · PDBe 7L5X · UniProt P55072

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