Research workbench

Apo-form cyclic trinucleotide synthase cdnd

Analyse Apo-form cyclic trinucleotide synthase cdnd in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 7D48
Type: protein
Length: 355 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Cyclic AMP-AMP-gmp synthase
EC: 2.7.7.-
UniProt: P0DSP4
Ligands: NA
Pockets: 2 · best druggability 0.71

Structure

x-ray diffraction · 1 distinct chain · 47% helix, 12% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Cyclic AMP-AMP-gmp synthase (EC 2.7.7.-)	protein	355	47% helix, 12% strand	P0DSP4

Ligands and binding sites

NA · Sodium ion · metal · chains A

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

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	768	0.71	0.77	56	empty
2	87	0.36	0.76	15	empty

Compared structures

7D48 · apo-form cyclic trinucleotide synthase CdnD · the same entry in another collection · chain A against A, TM-score 1.00
P0DSP4 · AlphaFold monomer V2.0 prediction for cyclic AMP-AMP-gmp synthase (P0DSP4) · a predicted model of the same protein · chain A against A, TM-score 0.98

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 P0DSP4
Elsewhere: RCSB PDB 7D48 · PDBe 7D48 · UniProt P0DSP4

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