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Crystal structure of a psychrophilic cca-adding enzyme determined by sad phasing

Analyse Crystal structure of a psychrophilic cca-adding enzyme determined by sad phasing in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 7OTR
Type: protein
Length: 373 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Cca-adding protein
UniProt: A0A1C7DQ98
Ligands: PO4
Pockets: 1 · best druggability 0.63

Structure

x-ray diffraction · 1 distinct chain · 55% helix, 11% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Cca-adding protein	protein	373	55% helix, 11% strand	A0A1C7DQ98

Ligands and binding sites

PO4 · Phosphate ion · ion · 2 copies · chains A
ACT · Acetate ion · additive · 3 copies · chains A
GOL · Glycerol · additive · 2 copies · chains A
TRS · 2-amino-2-hydroxymethyl-propane-1,3-diol · 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	417	0.63	0.78	39	PO4, ACT, TRS

Compared structures

7OTR · Crystal structure of a psychrophilic CCA-adding enzyme determined by SAD phasing · 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 A0A1C7DQ98
Elsewhere: RCSB PDB 7OTR · PDBe 7OTR · UniProt A0A1C7DQ98

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