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Crystal structure of peptidase E with ordered active site loop from salmonella enterica

Analyse Crystal structure of peptidase E with ordered active site loop from salmonella… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6A4S
Type: protein
Length: 465 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Peptidase E
EC: 3.4.13.21
UniProt: P36936
Pockets: 4 · best druggability 0.81

Structure

x-ray diffraction · 2 distinct chains · 30% helix, 22% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Peptidase E (EC 3.4.13.21)	protein	235	29% helix, 22% strand	P36936
B	Peptidase E (EC 3.4.13.21)	protein	230	31% helix, 22% strand	P36936

Pockets

4 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	222	0.81	0.94	33	empty
2	206	0.54	0.79	23	empty
3	226	0.53	0.77	25	empty
4	50	0.25	0.73	19	empty

Interfaces

1 interface between chains.

A–B · 1712 Å² buried · 12 hydrogen bonds · protein-protein

Compared structures

6A4S · Crystal structure of peptidase E with ordered active site loop from Salmonella enterica · the same entry in another collection · chain A against A, TM-score 1.00
P36936 · AlphaFold monomer V2.0 prediction for peptidase E (P36936) · a predicted model of the same protein · chain B against A, TM-score 0.99

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 P36936
Elsewhere: RCSB PDB 6A4S · PDBe 6A4S · UniProt P36936

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