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P97-R155H mutant dodecamer I

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

PDB: 7L5W
Type: protein
Length: 6,636 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 0.85

Structure

electron microscopy · 1 distinct chain · 46% 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	553	46% 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	788	0.85	0.88	118	empty
2	1023	0.85	0.86	140	empty
3	1046	0.85	0.86	136	empty
4	1065	0.85	0.86	141	empty
5	972	0.85	0.86	117	empty

Interfaces

25 interfaces between chains.

E–F · 3759 Å² buried · 34 hydrogen bonds · protein-protein
C–D · 3748 Å² buried · 39 hydrogen bonds · protein-protein
G–L · 3748 Å² buried · 34 hydrogen bonds · protein-protein
I–J · 3747 Å² buried · 37 hydrogen bonds · protein-protein
A–B · 3744 Å² buried · 35 hydrogen bonds · protein-protein

Compared structures

7L5W · p97-R155H mutant dodecamer I · 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 7L5W · PDBe 7L5W · UniProt P55072

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