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Crystal structure of drosophila alpha methyldopa-resistant PROTEIN/3, 4-dihydroxyphenylacetaldehyde synthase

Analyse Crystal structure of drosophila alpha methyldopa-resistant PROTEIN/3… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6JRL
Type: protein
Length: 465 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: 3,4-dihydroxyphenylacetaldehyde synthase
EC: 1.13.12.15
UniProt: P18486
Pockets: 3 · best druggability 0.49

Structure

x-ray diffraction · 1 distinct chain · 51% helix, 14% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	3,4-dihydroxyphenylacetaldehyde synthase (EC 1.13.12.15)	protein	465	51% helix, 14% strand	P18486

Pockets

3 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	244	0.49	0.73	22	empty
2	127	0.42	0.76	23	empty
3	54	0.28	0.74	13	empty

Modifications

Observed in the structure: 1 modified (cofactor).

Compared structures

6JRL · Crystal structure of Drosophila alpha methyldopa-resistant… · the same entry in another collection · chain A against A, TM-score 1.00
P18486 · AlphaFold monomer V2.0 prediction for 3,4-dihydroxyphenylacetaldehyde synthase (P18486) · 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 P18486
Elsewhere: RCSB PDB 6JRL · PDBe 6JRL · UniProt P18486

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