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Crystal structure of protein CC_0490 from caulobacter crescentus, pfam DUF152

Analyse Crystal structure of protein CC_0490 from caulobacter crescentus, pfam DUF152 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1XFJ
Type: protein
Length: 256 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Conserved hypothetical protein
UniProt: Q9AAV3
Pockets: 1 · best druggability 0.51

Structure

x-ray diffraction · 1 distinct chain · 29% helix, 27% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Conserved hypothetical protein	protein	256	29% helix, 27% strand	Q9AAV3

Ligands and binding sites

ACT · Acetate ion · additive · chains A
BME · Beta-mercaptoethanol · additive · chains A
GOL · Glycerol · 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	177	0.51	0.78	30	BME

Modifications

Observed in the structure: 2 modified, 1 covalent (engineered, additive adduct).

Compared structures

1XFJ · Crystal structure of protein CC_0490 from Caulobacter crescentus, Pfam DUF152 · 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 Q9AAV3
Elsewhere: RCSB PDB 1XFJ · PDBe 1XFJ · UniProt Q9AAV3

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