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Structure of a psychrophilic cca-adding enzyme in complex with cmpcpp at room temperature in chipx microfluidic device

Analyse Structure of a psychrophilic cca-adding enzyme in complex with cmpcpp at room… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6Q52
Type: protein
Length: 366 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Cca-adding enzyme
EC: 2.7.7.72
UniProt: A0A1C7DQ98
Ligands: 2TM
Pockets: 1 · best druggability 0.58

Structure

x-ray diffraction · 1 distinct chain · 55% helix, 10% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Cca-adding enzyme (EC 2.7.7.72)	protein	366	55% helix, 10% strand	A0A1C7DQ98

Ligands and binding sites

2TM · 5'-O-[(S)-hydroxy{[(s)-hydroxy(phosphonooxy) phosphoryl]methyl}phosphoryl]cytidine · ligand · 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	356	0.58	0.76	31	2TM

Compared structures

6Q52 · Structure of a psychrophilic CCA-adding enzyme in complex with CMPcPP at room temperature… · 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 6Q52 · PDBe 6Q52 · UniProt A0A1C7DQ98

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