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Rameb complex of cyclodextrin glycosyltransferase mutant

Analyse Rameb complex of cyclodextrin glycosyltransferase mutant in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 7CGT
Type: protein
Length: 684 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Cyclodextrin glycosyltransferase
EC: 2.4.1.19
UniProt: P30920
Ligands: CA
Pockets: 3 · best druggability 0.77

Structure

x-ray diffraction · 1 distinct chain · 21% helix, 31% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Cyclodextrin glycosyltransferase (EC 2.4.1.19)	protein	684	21% helix, 31% strand	P30920

Ligands and binding sites

CA · Calcium ion · metal · 2 copies · chains A

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

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	475	0.77	0.85	68	empty
2	396	0.63	0.78	29	empty
3	147	0.40	0.74	25	empty

Modifications

Observed in the structure: 1 disulfide (disulfide).

Compared structures

7CGT · Rameb complex of cyclodextrin glycosyltransferase mutant · the same entry in another collection · chain A against A, TM-score 1.00
P30920 · AlphaFold monomer V2.0 prediction for cyclomaltodextrin glucanotransferase (P30920) · a predicted model of the same protein · 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 P30920
Elsewhere: RCSB PDB 7CGT · PDBe 7CGT · UniProt P30920

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