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Structure of pro-esp mutant- S66V

Analyse Structure of pro-esp mutant- S66V in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6Q12
Type: protein
Length: 406 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Glutamyl endopeptidase
EC: 3.4.21.19
UniProt: P0C0Q2
Pockets: 1 · best druggability 0.41

Structure

x-ray diffraction · 2 distinct chains · 13% helix, 42% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Glutamyl endopeptidase (EC 3.4.21.19)	protein	204	13% helix, 42% strand	P0C0Q2
B	Glutamyl endopeptidase (EC 3.4.21.19)	protein	202	13% helix, 42% strand	P0C0Q2

Pockets

1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	156	0.41	0.74	22	empty

Interfaces

1 interface between chains.

A–B · 59 Å² buried · 0 hydrogen bonds · protein-protein

Compared structures

6Q12 · Structure of pro-Esp mutant- S66V · the same entry in another collection · chain A against A, TM-score 1.00
P0C0Q2 · AlphaFold monomer V2.0 prediction for glutamyl endopeptidase (P0C0Q2) · a predicted model of the same protein · 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 P0C0Q2
Elsewhere: RCSB PDB 6Q12 · PDBe 6Q12 · UniProt P0C0Q2

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