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Crystal structure of a beta-barrel like protein (ABAYE2633) from acinetobacter baumannii aye at 1.43 a resolution

Analyse Crystal structure of a beta-barrel like protein (ABAYE2633) from acinetobacter… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4PUX
Type: protein
Length: 157 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Uncharacterized protein
UniProt: B0VAD0
Ligands: CL
Pockets: 1 · best druggability 0.67

Structure

x-ray diffraction · 1 distinct chain · 8% helix, 56% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Uncharacterized protein	protein	157	8% helix, 56% strand	B0VAD0

Ligands and binding sites

CL · Chloride ion · ion · 5 copies · chains A
EDO · 1,2-ethanediol · additive · 4 copies · chains A
CIT · Citric acid · additive · 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	135	0.67	0.88	27	EDO, CL

Modifications

Observed in the structure: 2 modified (engineered).

Compared structures

4PUX · Crystal structure of a beta-barrel like protein (ABAYE2633) from Acinetobacter baumannii… · 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 B0VAD0
Elsewhere: RCSB PDB 4PUX · PDBe 4PUX · UniProt B0VAD0

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