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Full length structure of cystathionine beta-synthase from drosophila

Analyse Full length structure of cystathionine beta-synthase from drosophila in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3PC2
Type: protein
Length: 500 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: CG1753, isoform a
EC: 4.2.1.22
UniProt: Q9VRD9
Ligands: HEM, PLP
Pockets: 6 · best druggability 0.78

Structure

x-ray diffraction · 1 distinct chain · 36% helix, 18% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	CG1753, isoform a (EC 4.2.1.22)	protein	500	36% helix, 18% strand	Q9VRD9

Ligands and binding sites

HEM · Protoporphyrin IX containing Fe · ligand · chains A
PLP · Pyridoxal-5'-phosphate · ligand · chains A

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

Pockets

6 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	1063	0.78	0.80	77	empty
2	54	0.70	0.98	23	PLP
3	314	0.60	0.78	51	HEM
4	116	0.58	0.85	22	empty
5	107	0.46	0.79	17	empty

Modifications

Observed in the structure: 1 cofactor (pyridoxal phosphate Schiff base).

Compared structures

3PC2 · Full length structure of cystathionine beta-synthase from Drosophila · 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 Q9VRD9
Elsewhere: RCSB PDB 3PC2 · PDBe 3PC2 · UniProt Q9VRD9

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