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Crystal structure of vibrio cholerae putative NTPase epse

Analyse Crystal structure of vibrio cholerae putative NTPase epse in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1P9R
Type: protein
Length: 378 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: General secretion pathway protein E
UniProt: P37093
Ligands: ZN, CL
Pockets: 1 · best druggability 0.64

Structure

x-ray diffraction · 1 distinct chain · 38% helix, 27% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	General secretion pathway protein E	protein	378	38% helix, 27% strand	P37093

Ligands and binding sites

ZN · Zinc ion · metal · chains A
CL · Chloride ion · ion · chains A

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

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	416	0.64	0.78	44	CL

Modifications

Observed in the structure: 11 modified (engineered).

Compared structures

1P9R · Crystal Structure of Vibrio cholerae putative NTPase EpsE · the same entry in another collection · chain A against A, TM-score 1.00
P37093 · AlphaFold monomer V2.0 prediction for type II secretion system ATPase E (P37093) · a predicted model of the same protein · chain A against A, TM-score 0.85

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 P37093
Elsewhere: RCSB PDB 1P9R · PDBe 1P9R · UniProt P37093

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